Class / Patent application number | Description | Number of patent applications / Date published |
530327000 | 11 to 14 amino acid residues in defined sequence | 75 |
20080249283 | Hla-Binding Peptides, Precursors Thereof, Dna Fragments and Recombinant Vectors that Code for Those Peptide Sequences - An HLA-binding peptide binding to an HLA-A type molecule, said HLA-binding peptide comprising at least one type of amino acid sequence selected from the group consisting of SEQ ID NOS: 1 to 183, and not less than 8 and not more than 11 amino acid residues is provided. Any of the amino acid sequence is predicted to have the binding property to a HLA-A type molecule by a predicting program using an active learning experiment method as illustrated in FIG. | 10-09-2008 |
20080293916 | Hla-Binding Peptide, and Dna Fragment and Recombinant Vector Coding for Said Hla-Binding Peptide - An HLA-binding peptide binding to an HLA-A type molecule, said HLA-binding peptide comprising at least one type of amino acid sequence selected from the group consisting of SEQ ID NOS: 1 to 60, and not less than 8 and not more than 11 amino acid residues is provided. Any of the amino acid sequence is predicted to have the binding property to a human HLA-A24 molecule or a human HLA-A2 molecule by a predicting program using an active learning experiment method as illustrated in FIG. | 11-27-2008 |
20080293917 | Peptide Purification By Means Of Metal Ion Affinity Chromatography - A polymer substrate functionalized with a functionality comprising at least one cyclic, metal ion coordinating ligand group, the cyclic ligand group comprising at least 3 metal ion coordinating donor atoms independently selected from the group consisting of N, O and S. | 11-27-2008 |
20080306243 | Hla-Binding Peptide, and Dna Fragment and Recombinant Vector Coding for Said Hla-Binding Peptide - An HLA-binding peptide binding to an HLA-A type molecule is provided that includes at least one type of amino acid sequence selected from the group consisting of SEQ ID NOS: 1 to 30, and not less than 8 and not more than 11 amino acid residues. All of these amino acid sequences are amino acid sequences predicted to bind to a human HLA-A molecule using a prediction program employing an active learning experiment method shown in FIG. | 12-11-2008 |
20090005534 | Methods and Compositions for the Treatment of Gastrointestinal Disorders - The present invention features compositions and related methods for treating IBS and other gastrointestinal disorders and conditions (e.g., gastrointestinal motility disorders, functional gastrointestinal disorders, gastroesophageal reflux disease (GERD), Crohn's disease, ulcerative colitis, Inflammatory bowel disease, functional heartburn, dyspepsia (including functional dyspepsia or nonulcer dyspepsia), gastroparesis, chronic intestinal pseudo-obstruction (or colonic pseudo-obstruction), and disorders and conditions associated with constipation, e.g., constipation associated with use of opiate pain killers, post-surgical constipation, and constipation associated with neuropathic disorders as well as other conditions and disorders using peptides and other agents that activate the guanylate cyclase C (GC-C) receptor. | 01-01-2009 |
20090023894 | Neutralizing Antibody Against HGF - The neutralizing antibody against HGF binding to the inventive neutralizable epitope of HGF is capable of neutralizing HGF as a single agent, and can be effectively used for preventing and treating intractable diseases and cancers that are caused by binding of HGF to its receptor Met. | 01-22-2009 |
20090023895 | HLA-BINDING PEPTIDE, PRECURSOR THEREOF, AND DNA FRAGMENT AND RECOMBINANT VECTOR CODING FOR SAID HLA-BINDING PEPTIDE - An HLA-binding peptide binding to an HLA-A type molecule is provided that includes one or more types of amino acid sequence selected from the group consisting of SEQ ID NOS: 1 to 52, and not less than 8 and not more than 11 amino acid residues. All of these amino acid sequences are amino acid sequences predicted to bind to a human HLA-A molecule using a prediction program employing an active learning experiment method shown in FIG. | 01-22-2009 |
20090062512 | Comparative ligand mapping from MHC class I positive cells - The present invention relates generally to a methodology for the isolation, purification and identification of peptide ligands presented by MHC positive cells. In particular, the methodology of the present invention relates to the isolation, purification and identification of these peptide ligands from soluble class I and class II MHC molecules which may be from uninfected, infected, or tumorigenic cells. The methodology of the present invention broadly allows for these peptide ligands and their cognate source proteins thereof to be identified and used as markers for infected versus uninfected cells and/or tumorigenic versus nontumorigenic cells, with said identification being useful for marking or targeting a cell for therapeutic treatment or priming the immune response against infected/tumorigenic cells. | 03-05-2009 |
20090143567 | MULTIBLOCK COPOLYMERS HAVING IMPROVED MECHANICAL PROPERTIES - Replacement of the amorphous peptide domain of a structural biopolymer, such as silk from silkworms or spiders, with a nonpeptide segment while maintaining the β-sheet forming crystalline segments provides synthetic multiblock copolymers having solid-state structures and mechanical properties similar to the naturally occurring structural biopolymer is described herein. Such synthetic multiblock copolymers may be produced as films or fibers. | 06-04-2009 |
20090176966 | Natural IGM Antibodies and Inhibitors Thereof - The invention provides natural IgM antibody inhibitors that may be used to treat various inflammatory diseases or disorders. | 07-09-2009 |
20090281278 | MODIFIED MOLECULES WHICH PROMOTE HEMATOPOIESIS - The present disclosure relates to modified EPO mimetic peptides having specific properties. | 11-12-2009 |
20100016549 | PEYER'S PATCH AND/OR M-CELL TARGETING LIGANDS - Purified synthetic polypeptide ligands for targeting pharmaceutical agents and carriers comprising such agents to intestinal epithelial tissue, especially Peyer's patch and/or M-Cell tissue. Also methods of using the ligands. | 01-21-2010 |
20100063251 | COMPOSITIONS AND METHODS FOR TREATMENT OF CHRONIC FATIGUE SYNDROME AND NEURODEGENERATIVE DISEASES - The present invention relates to use of pharmaceutical formulations of a-MSH for the treatment of chronic fatigue syndrome and neurodegenerative diseases. | 03-11-2010 |
20100081787 | PEPTIDES AND PEPTIDOMIMETIC COMPOUNDS, THE MANUFACTURING THEREOF AS WELL AS THEIR USE FOR PREPARING A THERAPEUTICALLY AND/OR PREVENTIVELY ACTIVE PHARMACEUTICAL COMPOSITION - Peptides, peptidomimetics and derivatives thereof of the general formula I: | 04-01-2010 |
20100081788 | Process for the Preparation of Pramlintide - The present invention provides for an efficient process for making Pramlinitide, as well as novel intermediates for the making of the same. | 04-01-2010 |
20100099845 | PROTECTED ENANTIOPURE TRIFLUOROTHREONINES AND METHODS OF MAKING AND USING SAME - Disclosed are processes for preparing a protected trifluorothreonine, or salt thereof or carboxylate derivative thereof, the process comprising: dihydroxylation of an alkene to yield a dihydroxyl compound; conversion of the dihydroxyl compound to a monohydroxyl compound; protection of the monohydroxyl compound to yield an azide compound; transformation of the azide compound to yield an amino compound; protection of the amino compound to yield a protected amine compound; and oxidation of the protected amine compound to yield the protected trifluorothreonine. Also disclosed are compounds having the structure: | 04-22-2010 |
20100168383 | Skin or Hair Binding Peptides - The invention is directed to peptides. Specifically, the invention is directed to peptides which bind skin and do not bind hair. Alternatively, the invention is drawn to peptides which bind hair and do not bind skin. | 07-01-2010 |
20100197891 | METHOD FOR PEPTIDE SYNTHESIS - A new method of anchoring a growing peptide chain during chemical synthesis to a solid-phase support is devised. Novel amino acid derivatives and peptide derivatives, both unbonded and bonded to a solid-phase support, are also provided. | 08-05-2010 |
20100261877 | PROCESS FOR ISOLATING THERAPEUTIC PEPTIDES - Disclosed are methods of isolating linaclotide, a cyclized 14-amino-acid peptide with three disulfide bonds. The sequence consists of Cys-Cys-Glu-Tyr-Cys-Cys-Asn-Pro-Ala-Cys-Thr-Gly-Cys-Tyr with disulfide bridges between the cysteine residues at positions 1 and 6, 2 and 10, and 5 and 13. The drug acts as a GCC superagonist, elevating intracellular cGMP composition for treating various disorders, including gastrointestinal disorders, obesity, congestive heart failure and benign prostatic hyperplasia. | 10-14-2010 |
20100280220 | Gold binding peptides and shape-and size-tunable synthesis of gold nanostructures - The present invention relates to gold binding peptides and shape- and size-tunable synthesis of gold nanostructures. The present inventions are very useful for the production of well-designed, gold-based architectures. The size- and shape-specific gold nanostructure materials prepared by the present invention may find use as: highly conductive interconnections for single-electron transistors, catalysts for the oxidation of carbon monoxide; biological and chemical sensors; and as contrasting agents for electron microscopic and medical imaging applications. | 11-04-2010 |
20100286368 | NOVEL POLYPEPTIDE AND PROCESS FOR PRODUCING THE SAME - The present invention provides a novel polypeptide or polypeptide derivative which has no risk of infection with a pathogen or propagation of a pathogenic factor and of an undesirable side effect, and which is useful as a carrier of various biologically-active substances or apatite, as well as a process for producing the same. More particularly, the present invention provides a polypeptide comprising a peptide unit having an amino acid sequence represented by the formula: -Pro-X-Gly- (wherein X represents Pro or Hyp) and a peptide unit having an amino acid sequence represented by the formula: -Pro-Hyp(O—Y—Z)-Gly- (wherein Y represents a carbonyl group, a saturated or unsaturated hydrocarbon group with or without a carbonyl group, or a saturated or unsaturated hydrocarbon group with or without a carbonyl group, including an aromatic group, and Z represents a carboxyl group), as well as a process for producing the same. | 11-11-2010 |
20100292437 | Polypeptides useful for appetite suppression - The present invention relates to polypeptides obtained from bear derivative isolate which are useful in suppressing appetite. The polypeptides of the present invention are most preferably between 12 and 13 amino acid residues in length and a mass of about 1249. The present invention also relates to a method of treating obesity by administering to obese subjects an effective amount of the polypeptides of the present invention. | 11-18-2010 |
20100292438 | PROTEINACEOUS COMPOUNDS - A purified novel peptide micrin and its fragments are disclosed. The molecule has hormonal functions and has wide-ranging biological effects. Several uses are disclosed including its therapeutic potential in tissue reduction, tumour suppression, infertility and senescence. A micrin-recognising antibody and the micrin gene are also disclosed. | 11-18-2010 |
20110060124 | HLA-BINDING PEPTIDES, PRECURSORS THEREOF, DNA FRAGMENTS AND RECOMBINANT VECTORS THAT CODE FOR THOSE PEPTIDE SEQUENCES - An HLA-binding peptide binding to an HLA-A type molecule, said HLA-binding peptide comprising at least one type of amino acid sequence selected from the group consisting of SEQ ID NOS: 1 to 183, and not less than 8 and not more than 11 amino acid residues is provided. Any of the amino acid sequences is predicted to have the binding property to a human HLA-A type molecule by a predicting program using an active learning experiment method as illustrated in FIG. | 03-10-2011 |
20110065896 | POLYETHER POLYOL DENDRON CONJUGATES WITH EFFECTOR MOLECULES FOR BIOLOGICAL TARGETING - Subject of the present invention are polyether polyol dendron conjugates comprising a specific polyether polyol dendron moiety, at least one certain fluorescent effector molecule (E). Such polyether polyol dendron conjugates may be used for diagnostic and therapeutic purposes, whereby the optical properties of the at least one certain fluorescent effector molecule are enhanced due to the attachment to the polyether polyol dendron conjugate. | 03-17-2011 |
20110077381 | NOVEL NPR-B AGONISTS - Disclosed are novel compounds having NPR-B agonistic activity. Preferred compounds are linear peptides containing 8-13 conventional or non-conventional L- or D-amino acid residues connected to one another via peptide bonds. | 03-31-2011 |
20110087004 | ENHANCED ORAL TRANSCOMPARTMENTAL DELIVERY OF THERAPEUTIC OR DIAGNOSTIC AGENTS - The invention is directed to pharmaceutical compositions and methods for delivery of a therapeutic or diagnostic agent from one bodily compartment to one or more other bodily compartment by administering one of the following conjugates: a polymer having multiple functional groups at least one of which is covalently bound to a therapeutic or diagnostic agent, and at least one cell uptake promoter covalently bound to the therapeutic or diagnostic agent; or a polymer and at least one cell uptake promoter bound thereto; the polymer further comprising multiple functional groups at least one of which is covalently bound a therapeutic or diagnostic agent. | 04-14-2011 |
20110087005 | HLA-BINDING PEPTIDE, PRECURSOR THEREOF, AND DNA FRAGMENT AND RECOMBINANT VECTOR CODING FOR SAID HLA-BINDING PEPTIDE - An HLA-binding peptide binding to an HLA-A type molecule is provided that includes one or more types of amino acid sequence selected from the group consisting of SEQ ID NOS: 1 to 52, and not less than 8 and not more than 11 amino acid residues. All of these amino acid sequences are amino acid sequences predicted to bind to a human HLA-A molecule using a prediction program employing an active learning experiment method shown in FIG. | 04-14-2011 |
20110092671 | Peptide manufacturing process - A process for the manufacture of peptide Omiganan in solution phase. Novel intermediates in the process for the manufacture of Omiganan and processes for the manufacture of these intermediates. | 04-21-2011 |
20110178270 | T-CELL DEATH-INDUCING EPITOPES - Cell death-inducing epitopes and polypeptides containing same. Also disclosed are compounds for inducing death of activated T-cells, a method of producing antibodies to the epitopes, a method of identifying compounds that bind to the epitopes, a method of inducing death of activated T-cells, and pharmaceutical compositions containing the compounds. | 07-21-2011 |
20110263817 | METAL-BINDING COMPOUNDS AND USES THEREFOR - The invention provides a method of reducing the damage done by reactive oxygen species (ROS) in an animal. The invention also provides a method of reducing the concentration of a metal in an animal. These methods comprise administering to the animal an effective amount of a metal-binding compound as further described in the application. The invention further provides a method of reducing the damage done by ROS to a cell, a tissue or an organ that has been removed from an animal. This method comprising contacting the cell, tissue or organ with a solution or medium containing an effective amount of a metal-binding compound of the invention. The invention further provides novel metal-binding compounds, pharmaceutical compositions comprising the metal-binding compounds, and kits comprising a container holding a metal-binding compound of the invention. | 10-27-2011 |
20110263818 | Peptidic Constructs with Amino Acid Surrogates - Peptidic constructs including at least one ring-constrained amino acid surrogate of formula I: | 10-27-2011 |
20110288270 | COMPARATIVE LIGAND MAPPING FROM MHC CLASS I POSITIVE CELLS - The present invention relates generally to a methodology for the isolation, purification and identification of peptide ligands presented by MHC positive cells. In particular, the methodology of the present invention relates to the isolation, purification and identification of these peptide ligands from soluble class I and class II MHC molecules which may be from uninfected, infected, or tumorigenic cells. The methodology of the present invention broadly allows for these peptide ligands and their cognate source proteins thereof to be identified and used as markers for infected versus uninfected cells and/or tumorigenic versus nontumorigenic cells, with said identification being useful for marking or targeting a cell for therapeutic treatment or priming the immune response against infected/tumorigenic cells. | 11-24-2011 |
20120077958 | Multimodal Imaging of Fibrin - Fibrin-specific imaging agents that contain at least two imaging reporters are described, as well as methods of making and using the contrast agents. | 03-29-2012 |
20120289681 | CONJUGATES OF CELL-PENETRATING PEPTIDES AND PHOSPHORESCENT METALLOPORPHYRINS FOR INTRACELLULAR OXYGEN MEASUREMENT - A phosphorescent compound of general Formula I, | 11-15-2012 |
20130023645 | METHODS FOR THE SYNTHESIS OF DICARBA BRIDGES IN ORGANIC COMPOUNDS - The present invention related to methods for forming dicarba bridges in organic compounds. This involves the use of a pair of complementary metathesisable groups on the organic compound, and subjecting the compound to cross-metathesis under microwave radiation conditions. In an alternative, the compounds containing a turn-induced group between the pair of cross metathesisable groups to facilitate the cross-metathesis. | 01-24-2013 |
20130085261 | BINDING PARTNERS OF ANTIBODIES SPECIFIC FOR DENDRITIC CELL ANTIGENS - The present invention relates to the field of diagnostics, therapeutics and immunological reagents. More particularly, the present invention provides binding partners of antibodies specific for dendritic cell (DC) antigens. The present invention further provides diagnostic and/or therapeutic agent based on the binding partners or antibodies specific for the binding partners. | 04-04-2013 |
20130102757 | METHODS FOR SELECTIVE TARGETING - A selective targeting method is disclosed comprising contacting a library of ligands, particularly a peptide library, with an anti-target to allow the ligands to bind to the anti-target; separating the non-binding ligands from the anti-target bound ligands, contacting the non-binding anti-target ligands with a target allowing the unbound ligands to bind with the target to form a target-bound ligand complex; separating the target-bound ligand complex from ligands which do not bind to the target, and identifying the target-bound ligands on the target-bound ligand complex wherein the target-bound ligands have a K | 04-25-2013 |
20130102758 | EZRIN ASSAY METHOD FOR THE IN VITRO DIAGNOSIS OF COLORECTAL CANCER - A method for the in vitro diagnosis of colorectal cancer by determining the presence of the Ezrin tumor marker in a biological sample taken from a patient suspected of having colorectal cancer using at least one anti-Ezrin monoclonal antibody directed against an Ezrin epitope chosen from the epitopes of sequence SEQ ID No.1, SEQ ID No.2, SEQ ID No.3, SEQ ID No.4+SEQ ID No.5, SEQ ID No.6+SEQ ID No.7 and SEQ ID No.8. Said method can be used for early diagnosis, screening, therapeutic follow-up and prognosis, and also for relapse diagnosis in relation to colorectal cancer. | 04-25-2013 |
20130109834 | HIGH SALT-RESISTANCE ANTIBACTERIAL PEPTIDE AND METHOD FOR PRODUCING THE SAME | 05-02-2013 |
20130131314 | Peptide Derivatives for Biofunctionalization of Silicon Substrates and Their Applications - The present invention relates to the use of a peptide consisting of 5 to 30 amino acid residues comprising an amino acid sequence selected from LLADTTHHRPWT (SEQ ID NO: 1), SPGLSLVSHMQT (SEQ ID NO: 2), and the sequences presenting at least 80% identity with SEQ ID NO: 1 or SEQ ID NO: 2, for the funcfionalization of silicon substrate. The present invention also relates to the specific peptides as such, and to silicon substrates functionalized by the adsorption on their surface of such specific peptides. Finally, the present invention is also directed to a process for the preparation of such functionalized silicon substrates, and to articles comprising a silicon substrate according to the invention. | 05-23-2013 |
20130281660 | DETECTION OF DEGRADATIVE ANZYMES AND BIOMOLECULES IN BODILY FLUIDS - Provided herein are compositions useful in detecting degradative enzymes and biomolecules in bodily fluid samples. | 10-24-2013 |
20130303728 | LIGAND AND METAL COMPLEX HAVING THE SAME - A ligand and a metal complex having the ligand are provided. The ligand and a paramagnetic metal ion form a metal complex with high stability, high relaxivity and high biocompatibility. The metal complex of the present invention is applicable to the preparation of MRI contrast agents for detecting atherosclerosis. The MRI contrast agent includes a peptide sequence specific to a matrix metalloprotease, and can be recognized by a pathological thrombocyte to target a specific site, so as to enhance the imaging contrast. | 11-14-2013 |
20130338340 | Peptides Having Antimicrobial Activity - Disclosed herein is a peptide for inhibiting growth of bacterial pathogens in a biological sample, characterized by an amino acid sequence selected from a group consisting of Pro-His-Trp-Trp-Lys-Trp-Ala-Trp-Trp-His-His-Arg-Arg (SEQ ID NO:1), Lys-His-Trp-Trp-Lys-His-Asp-Trp-Trp-Arg-Trp-Arg-Arg (SEQ ID NO:2), and Ile-Leu-Trp-Trp-Leu-Leu-Ala-Trp-Trp-Arg-Trp-Pro-His (SEQ ID NO:3). | 12-19-2013 |
20130338341 | Peptides Having Antimicrobial Activity - Disclosed herein is a peptide for inhibiting growth of bacterial pathogens in a biological sample, characterized by an amino acid sequence selected from a group consisting of Gly-Leu-Phe-Asp-Lys-Trp-Ala-Trp-Trp-Arg-Trp-Arg-Arg (SEQ ID NO:1), Gly-Leu-Phe-Asp-Ile-Trp-Ala-Trp-Trp-Arg-Trp-Arg-Arg (SEQ ID NO:2), Gly-Leu-Phe-Asp-Ile-Trp-Lys-Trp-Trp-Arg-Trp-Arg-Arg (SEQ ID No:3), Gly-Leu-Phe-Asp-Ile-Trp-Lys-Lys-Trp-Arg-Trp-Arg-Arg (SEQ ID NO:4), and Gly-Leu-Phe-Asp-Ile-Trp-Lys-Lys-Leu-Arg-Trp-Arg-Arg (SEQ ID NO:5). | 12-19-2013 |
20130345394 | NOVEL NPR-B AGONISTS - Disclosed are novel compounds having NPR-B agonistic activity. Preferred compounds are linear peptides containing 8-13 conventional or non-conventional L- or D-amino acid residues connected to one another via peptide bonds. | 12-26-2013 |
20140039154 | PROTEIN DISULFIDE ISOMERASE ASSAY METHOD FOR THE IN VITRO DIAGNOSIS OF COLORECTAL CANCER - A method for the in vitro diagnosis of colorectal cancer that comprises determining the presence of the protein disulfide isomerase tumor marker in a biological sample taken from a patient suspected of having colorectal cancer using at least one anti-PDI monoclonal antibody directed against a PDI epitope chosen from the epitopes of sequence SEQ ID No.1, SEQ ID No.2, with an aromatic amino acid which is close in the three-dimensional structure of PDI and SEQ ID No.3. | 02-06-2014 |
20140080996 | SKIN OR HAIR BINDING PEPTIDES - The invention is directed to peptides. Specifically, the invention is directed to peptides which bind skin and do not bind hair. Alternatively, the invention is drawn to peptides which bind hair and do not bind skin. | 03-20-2014 |
20140080997 | NOVEL MITE ALLERGEN - A safe and efficient recombinant mite allergen is provided as a therapeutic agent or a diagnostic agent for mite allergic diseases, which contains no anaphylaxis-inducing impurities. The following recombinant protein (a) or (b) is provided: | 03-20-2014 |
20140206838 | COMPOSITIONS AND METHODS FOR RECOGNITION OF RNA USING TRIPLE HELICAL PEPTIDE NUCLEIC ACIDS - Peptide nucleic acids containing thymidine and 2-aminopyridine (M) nucleobases formed stable and sequence selective triple helices with double stranded RNA at physiologically relevant conditions. The M-modified PNA displayed unique RNA selectivity by having two orders of magnitude higher affinity for the double stranded RNAs than for the same DNA sequences. Preliminary results suggested that nucleobase-modified PNA could bind and recognize double helical precursors of microRNAs. | 07-24-2014 |
20140206839 | CROSS LINKED HYALURONIC ACID-SILK AND USES THEREOF - The present specification provides for methods for purifying fibroins, purified fibroins, methods of conjugating biological and synthetic molecules to fibroins, fibroins conjugated to such molecules, methods of making fibroin hydrogels, fibroin hydrogels and fibroin hydrogel formulations useful for a variety of medical uses, including, without limitation uses as bulking agents, tissue space fillers, templates for tissue reconstruction or regeneration, cell culture scaffolds for tissue engineering and for disease models, surface coating to improve medical device function, or drug delivery devices. | 07-24-2014 |
20140221610 | DISPERSION AND DETACHMENT OF CELL AGGREGATES - Compositions comprising a protein or isolated peptide, and methods using the same for preventing, dispersing or detaching a biofilm, are disclosed. | 08-07-2014 |
20140296483 | METHOD FOR REMOVING FMOC GROUP - The present invention relates to a method of removing an Fmoc group, including a step of mixing a compound represented by the formula (I): | 10-02-2014 |
20140364584 | SKIN OR HAIR BINDING PEPTIDES - The invention is directed to peptides. Specifically, the invention is directed to peptides which bind skin and do not bind hair. Alternatively, the invention is drawn to peptides which bind hair and do not bind skin. | 12-11-2014 |
20150073122 | PORPHYRIN-PEPTOID CONJUGATE AND THE PREPARATION PROCESS THEREOF - Disclosed are a porphyrin-peptoid conjugate and a method for preparing the same. The porphyrin-peptoid conjugate according to the present disclosure has porphyrins arranged face-to-face on a helical peptoid. The porphyrin-peptoid conjugate according to the present disclosure is a new-concept photosensitizing dye material wherein the distance, arrangement and number of porphyrins are controllable. Since the porphyrin-peptoid conjugate is monodisperse and has a precisely defined structure, selective decoration of dyes is easy and dyes can be arranged on the peptoid helix sequence and space specifically. Accordingly, a new high-efficiency photosensitizing dye molecule system having wide absorption spectrum including the visible and near-infrared range and high absorption coefficient can be prepared. | 03-12-2015 |
20150087807 | LIPOPOLYSACCHARIDE-TARGETED PEPTIDE MIMIC VACCINE AGAINST Q FEVER - A vaccine and method of vaccination for conferring immunity to Q fever is described. The vaccine comprises a polypeptide with a sequence of SLTWHKHELHRK (m1E41920) or SPPWHKHELHRK (m1E44), or at least 90% identity to m1E41920 or m1E44. Constructs are also provided for use in vaccination and treatment of Q fever. A method to identify and generate new vaccines to prevent diseases caused by intracellular Gram-negative bacteria is also described. | 03-26-2015 |
20150087808 | PROCESS FOR THE MANUFACTURE OF CYCLIC UNDECAPEPTIDES - The present invention relates to processes and intermediates useful for the manufacture of cyclic undecapeptides, such as Alisporivir. | 03-26-2015 |
20150094449 | DETECTION OF DEGRADATIVE ENZYMES AND BIOMOLECULES IN BODILY FLUIDS - Provided herein are compositions useful in detecting degradative enzymes and biomolecules in bodily fluid samples. | 04-02-2015 |
20150299257 | BIOACTIVE PEPTIDE COMPLEXES - The present invention refers to proteins and bioactive peptides with immunomodulating and antiviral activity. Present peptide complexes have three-dimensional structure and are described by the following structural formula (SEQ ID NO: 23): | 10-22-2015 |
20150307553 | SYNTHETIC ANALOGUES OF NEURAL REGENERATION PEPTIDES - Embodiments of this invention include synthetic compounds (NRP analogues) of peptides termed neural regeneration peptides (NRPs). NRP analogues are made by substituting amino acids in the native peptide sequence, modifying amino acids chemically, by replacing amino acids with synthetic moieties, by stabilizing β-turns, acetylation of terminal glycine residues or by cyclization. NRP analogues can be used to treat a variety of conditions involving degeneration of neural cells, and includes treating disorders of the nervous system, including peripheral neuropathy, multiple sclerosis, diabetic peripheral neuropathy, neurotoxin-induced neurodegeneration, and amyotrophic lateral sclerosis. | 10-29-2015 |
20150314009 | DUAL-ACTION, UNNATURAL PROLINE-RICH PEPTIDES AS ANTIBIOTIC AGENTS AND METHODS THEREOF - The present invention cationic amphiphilic polyproline helices (CAPHs) compounds having increased hydrophobicity and cellular internalization as antimicrobial agents. Antimicrobial compositions and methods of using the same are also provided. | 11-05-2015 |
20150337012 | EGFR-BINDING PEPTIDE - Provided are a substance capable of binding to EGFR specifically with a high affinity and a pharmaceutical agent containing the substance. A peptide which contains at least an amino acid sequence is represented by the formula (1), (2) or (3), as described in the specification, and is composed of 12 to 50 amino acids: | 11-26-2015 |
20160015838 | Vinylsulfone-based 18F-labeling Compositions and Methods and Uses Thereof - A thio-selective radioactive labeling agent has the following general formula: | 01-21-2016 |
20160046691 | Novel Epitope for Switching to TH2 Cell and Use Thereof - The present invention relates to a novel epitope to convert T cell to type 2 helper T (T | 02-18-2016 |
20160052966 | Compositions Containing, Methods Involving, and Uses of Non-Natural Amino Acid Linked Dolastatin Derivatives - Disclosed herein are non-natural amino acids and dolastatin analogs that include at least one non-natural amino acid, and methods for making such non-natural amino acids and polypeptides. The dolastatin analogs can include a wide range of possible functionalities, but typically have at least one oxime, carbonyl, dicarbonyl, and/or hydroxylamine group. Also disclosed herein are non-natural amino acid dolastatin analogs that are further modified post-translationally, methods for effecting such modifications, and methods for purifying such dolastatin analogs. Typically, the modified dolastatin analogs include at least one oxime, carbonyl, dicarbonyl, and/or hydroxylamine group. Further disclosed are methods for using such non-natural amino acid dolastatin analogs and modified non-natural amino acid dolastatin analogs, including therapeutic, diagnostic, and other biotechnology use. | 02-25-2016 |
20160052969 | TEMPLATES FOR CONTROLLING SYNTHESIS OF NANOPARTICLES INTO DISCRETE ASSEMBLIES - An approach to synthesizing and assembling nanoparticles into discrete, size-tunable, pre-designed architectures is realized in a single synthetic/process step. | 02-25-2016 |
20160060311 | Development of Protein-Based Biotherapeutics That Penetrates Cell-Membrane and Induces Anti-Lung Cancer Effect - Improved Cell-Permeable Suppressor of Cytokine Signaling (iCP-SOCS3) Proteins, Polynucleotides Encoding the Same, and Anti-Lung Cancer Compositions Comprising the Same - In principle, protein-based biotherapeutics offers a way to control biochemical processes in living cells under non-steady state conditions and with fewer off-target effects than conventional small molecule therapeutics. However, systemic protein delivery in vivo has been proven difficult due to poor tissue penetration and rapid clearance. Protein transduction exploits the ability of some cell-penetrating peptide (CPP) sequences to enhance the uptake of proteins and other macromolecules by mammalian cells. Previously developed hydrophobic CPPs, named membrane translocating sequence (MTS), membrane translocating motif (MTM) and macromolecule transduction domain (MTD), are able to deliver biologically active proteins into a variety of cells and tissues. Various cargo proteins fused to these CPPs have been used to test the functional and/or therapeutic efficacy of protein transduction. Previously, recombinant proteins consisting of suppressor of cytokine signaling 3 (CP-SOCS3) protein fused to the fibroblast growth factor (FGF) 4-derived MTM were developed to inhibit inflammation and apoptosis. However, CP-SOCS3 fusion proteins expressed in bacteria cells were hard to be purified in soluble form. To address these critical limitations, CPP sequences called advanced MTDs (aMTDs) have been developed in this art. The development of this art has been accomplished by (i) analyzing previous developed hydrophobic CPP sequences to identify specific critical factors (CFs) that affect intracellular delivery potential and (ii) constructing artificial aMTD sequences that satisfy for each critical factor. In addition, solubilization domains (SDs) have been incorporated into the aMTD-fused SOCS3 recombinant proteins to enhance solubility with corresponding increases in protein yield and cell-/tissue-permeability. These recombinant SOCS3 proteins fused to aMTD/SD having much higher solubility/yield and cell-/tissue-permeability have been named as improved cell-permeable SOCS3 (iCP-SOCS3) proteins. Previously developed CP-SOCS3 proteins fused to MTM were only tested or used as anti-inflammatory agents to treat acute liver injury. In the present art, iCP-SOCS3 proteins have been tested for use as anti-cancer agents in the treatment of neoplasia in lung. Since SOCS3 is frequently deleted in cancer cells and loss of SOCS3 promotes resistance to apoptosis and proliferation, we reasoned that iCP-SOCS3 could be used as a protein-based intracellular replacement therapy for the treatment of lung cancer. The results demonstrated in this art support this reasoning: treatment of human non-small cell lung carcinoma cells with iCP-SOCS3 results in reduced cancer cell viability, enhanced apoptosis. Furthermore, iCP-SOCS3 inhibited migration/invasion of lung cancer cells. In the present invention with iCP-SOCS3, where SOCS3 is fused to an empirically determined combination of newly developed aMTD and customized SD, macromolecule intracellular transduction technology (MITT) enabled by the advanced MTDs may provide novel protein therapy against lung cancer. | 03-03-2016 |
20160060312 | Development of Protein-Based Biotherapeutics That Penetrates Cell-Membrane and Induces Anti-Pancreatic Cancer Effect - Improved Cell-Permeable Suppressor of Cytokine Signaling (iCP-SOCS3) Proteins, Polynucleotides Encoding the Same, and Anti-Pancreatic Cancer Compositions Comprising the Same - In principle, protein-based biotherapeutics offers a way to control biochemical processes in living cells under non-steady state conditions and with fewer off-target effects than conventional small molecule therapeutics. However, systemic protein delivery in vivo has been proven difficult due to poor tissue penetration and rapid clearance. Protein transduction exploits the ability of some cell-penetrating peptide (CPP) sequences to enhance the uptake of proteins and other macromolecules by mammalian cells. Previously developed hydrophobic CPPs, named membrane translocating sequence (MTS), membrane translocating motif (MTM) and macromolecule transduction domain (MTD), are able to deliver biologically active proteins into a variety of cells and tissues. Various cargo proteins fused to these CPPs have been used to test the functional and/or therapeutic efficacy of protein transduction. The recombinant proteins consisting of suppressor of cytokine signaling 3 (CP-SOCS3) protein fused to the fibroblast growth factor (FGF) 4-derived MTM were developed to inhibit inflammation and apoptosis. However, CP-SOCS3 fusion proteins expressed in bacteria cells were hard to be purified in soluble form. To address these critical limitations, CPP sequences called advanced MTDs (aMTDs) have been developed in this art. This is accomplished by (i) analyzing previous developed hydrophobic CPP sequences to identify specific critical factors (CFs) that affect intracellular delivery potential and (ii) constructing artificial aMTD sequences that satisfy each critical factor. In addition, solubilization domains (SDs) have been incorporated into the aMTD-fused SOCS3 recombinant proteins to enhance solubility with corresponding increases in protein yield and cell-/tissue-permeability. These recombinant SOCS3 proteins fused to aMTD/SD having much higher solubility/yield and cell-/tissue-permeability have been named as improved cell-permeable SOCS3 (iCP-SOCS3) proteins. Previously developed CP-SOCS3 proteins fused to MTM were only tested or used as anti-inflammatory agents to treat acute liver injury. In the present art, iCP-SOCS3 proteins have been tested for use as anti-cancer agents in the treatment of pancreatic cancer. Since SOCS3 is frequently deleted in cancer cells and loss of SOCS3 promotes resistance to apoptosis and proliferation, we reasoned that iCP-SOCS3 could be used as a protein-based intracellular replacement therapy for the treatment of pancreatic cancer. The results demonstrated in this art support this reasoning: treatment of pancreatic cancer cells with iCP-SOCS3 results in reduced cancer cell viability, enhanced apoptosis and loss of cell migration/invasion potentials. Furthermore, iCP-SOCS3 inhibits the growth of pancreatic cancer in a subcutaneous xenografts model. In the present invention with iCP-SOCS3, where SOCS3 is fused to an empirically determined combination of newly developed aMTD and customized SD, macromolecule intracellular transduction technology (MITT) enabled by the advanced MTDs may provide novel protein therapy against pancreatic cancer. | 03-03-2016 |
20160060313 | Development of Protein-Based Biotherapeutics That Penetrates Cell-Membrane and Induces Anti-Angiogenic Effect - Improved Cell-Permeable Suppressor of Cytokine Signaling (iCP-SOCS3) Proteins, Polynucleotides Encoding the Same, and Anti-Angiogenic Compositions Comprising the Same - In principle, protein-based biotherapeutics offers a way to control biochemical processes in living cells under non-steady state conditions and with fewer off-target effects than conventional small molecule therapeutics. However, systemic protein delivery in vivo has been proven difficult due to poor tissue penetration and rapid clearance. Protein transduction exploits the ability of some cell-penetrating peptide (CPP) sequences to enhance the uptake of proteins and other macromolecules by mammalian cells. Previously developed hydrophobic CPPs—named membrane translocating sequence (MTS), membrane translocating motif (MTM) and macromolecule transduction domain (MTD)—are able to deliver biologically active proteins into a variety of cells and tissues. Various cargo proteins fused to these CPPs have been used to test the functional and/or therapeutic efficacy of protein transduction. Previously, recombinant proteins consisting of suppressor of cytokine signaling 3 (SOSC3) fused to the fibroblast growth factor (FGF) 4-derived MTM were developed to inhibit inflammation and apoptosis. However, this SOCS3 fusion proteins expressed in bacteria cells were hard to be purified in soluble form. To address these critical limitations, CPP sequences called advanced MTDs (aMTDs) have been developed in this art. The development of this art has been accomplished by (i) analyzing previous developed hydrophobic CPP sequences to identify specific critical factors (CFs) that affect intracellular delivery potential and (ii) constructing artificial aMTD sequences that satisfy each critical factor. Furthermore, solubilization domains (SDs) have been incorporated into the aMTD-fused SOCS3 recombinant proteins to enhance solubility with corresponding increases in protein yield and cell-/tissue-permeability. These recombinant SOCS3 proteins fused to aMTD/SD having much higher solubility/yield and cell-/tissue-permeability have been named as improved cell-permeable SOCS3 (iCP-SOCS3) proteins. Previously developed SOCS3 recombinant proteins fused to MTM were only tested or used as anti-inflammatory agents to treat acute liver injury. In the present art, iCP-SOCS3 proteins have been tested for use as anti-angiogenic agents. Since SOCS3 is known to be an endogenous inhibitor of pathological angiogenesis, we reasoned that iCP-SOCS3 could be used as a protein-based intracellular replacement therapy for inhibiting angiogenesis in tumor cells. The results demonstrated in this art support this following reasoning: Cancer treatment with iCP-SOCS3 results in reduced endothelial cell viability, loss of cell migration potential and suppressed vascular sprouting potentials. In the present invention with iCP-SOCS3, where SOCS3 is fused to an empirically determined combination of newly developed aMTD and customized SD, macromolecule intracellular transduction technology (MITT) enabled by the advanced MTDs may provide novel protein therapy against cancer cell-mediated angiogenesis. | 03-03-2016 |
20160060314 | Development of a Protein-Based Biotherapeutic Agent That Penetrates Cell-Membrane and Induces Anti-Tumor Effect in Solid Tumors - Improved Cell-Permeable Suppressor of Cytokine Signaling (iCP-SOCS3) Proteins, Polynucleotides Encoding the Same, and Anti-Tumor Compositions Comprising the Same - In principle, protein-based biotherapeutics offers a way to control biochemical processes in living cells under non-steady state conditions and with fewer off-target effects than conventional small molecule therapeutics. However, systemic protein delivery in vivo has been proven difficult due to poor tissue penetration and rapid clearance. Protein transduction exploits the ability of some cell-penetrating peptide (CPP) sequences to enhance the uptake of proteins and other macromolecules by mammalian cells. Previously developed hydrophobic CPPs, named membrane translocating sequence (MTS), membrane translocating motif (MTM) and macromolecule transduction domain (MTD), are able to deliver biologically active proteins into a variety of cells and tissues. Various cargo proteins fused to these CPPs have been used to test the functional and/or therapeutic efficacy of protein transduction. The recombinant proteins consisting of suppressor of cytokine signaling 3 (CP-SOCS3) protein fused to the fibroblast growth factor (FGF) 4-derived MTM were developed to inhibit inflammation and apoptosis. However, CP-SOCS3 fusion proteins expressed in bacteria cells were hard to be purified in soluble form. To address these critical limitations, CPP sequences called advanced MTDs (aMTDs) have been developed in this art. This is accomplished by (i) analyzing previous developed hydrophobic CPP sequences to identify specific critical factors (CFs) that affect intracellular delivery potential and (ii) constructing artificial aMTD sequences satisfied for each critical factor. In addition, solubilization domains (SDs) have been incorporated into the aMTD-fused SOCS3 recombinant proteins to enhance solubility with corresponding increases in protein yield and cell-/tissue-permeability. These recombinant SOCS3 proteins fused to aMTD/SD having much higher solubility/yield and cell-/tissue-permeability have been named as improved cell-permeable SOCS3 (iCP-SOCS3) proteins. Previously developed CP-SOCS3 proteins fused to MTM were only tested or used as anti-inflammatory agents to treat acute liver injury. In the present art, iCP-SOCS3 proteins have been tested for use as anti-cancer agents in the treatment of various cancers likes gastric, colorectal and breast cancer, and glioblastoma. Since SOCS3 is frequently deleted in and loss of SOCS3 in tumors promotes resistance to apoptosis and proliferation, we reasoned that iCP-SOCS3 could be used as a protein-based intracellular replacement therapy for the treatment of various cancers. The results demonstrated in this art support the reasoning: treatment of cancer cells with iCP-SOCS3 results in reduced cancer cell viability, enhanced apoptosis of solid tumors including gastric, colorectal and breast cancer, and glioblastoma and loss of cell migration/invasion potential. Furthermore, iCP-SOCS3 inhibits the growth of gastric and colorectal tumors in a subcutaneous xenografts model. In the present invention with iCP-SOCS3, where SOCS3 is fused to an empirically determined combination of newly developed aMTD and customized SD, macromolecule intracellular transduction technology (MITT) enabled by the advanced MTDs may provide novel protein therapy against various tumors such as gastric cancer, colorectal cancer, glioblastoma, and breast cancer. | 03-03-2016 |
20160060319 | Development of Protein-Based Biotherapeutics That Induced Osteogenesis for Bone Healing Therapy: Cell-Permeable BMP2 and BMP7 Recombinant Proteins (CP-BMP2 & CP-BMP7), Polynucleotides Encoding the Same and Pro-osteogenic Compositions Comprising the Same - The present invention is about direct protein delivery system for bone morphogenetic proteins (BMPs) to enhance bone regeneration without the need of additional delivery carrier which requires open surgery for their implantation. The cell-permeable BMP (CP-BMP) recombinant proteins are fused with advanced macromolecule transduction domain (aMTD) to give them ability for cell penetration and with solubilization domain (SD) to increase their solubility and manufacturing yield. Because existing BMP recombinant proteins have short half-life, they have been delivered with polymeric or inorganic vehicles for their sustained release. However, CP-BMPs fused to combination of aMTD and SD can easily and rapidly penetrate into the cytosol after treating on cells that likes hiding in a shelter from wash off in body fluid, and avoid rapid degradation. For the development of CP-BMP, BMP2 and BMP7 have been selected among various types of BMP family due to their potent osteo-inductivity. Both of proteins are produced in mature form (MP) as an active domain and pro-peptide form (latency associated peptide (LAP)+MP) for prolonged stability of proteins. In the present art, three strategic steps are used to prove the validity of using CP-BMPs on bone regeneration and new bone formation. First, randomly selected aMTDs and various types of SDs have been fused to BMP proteins for determine the best structural composition for highest solubility/yield and cell-/tissue-permeability. Next, aMTDs are fused to BMP2 and BMP7 proteins with optimized structure to determine the best construct for maximized cell- and tissue-permeability. Finally, biological activity of BMP2, BMP7 and combination of BMP2 and BMP7 recombinant proteins have been evaluated to enhance in vitro osteogenic differentiation and in vivo bone regeneration. The CP-BMPs can be applied to repair skeletal injuries which are by bone fracture, osteogenesis imperfecta, and bone extraction. | 03-03-2016 |
20160068570 | ANTI-TUMOR POLYPEPTIDES AND METHOD FOR PREPARING ANTI-TUMOR DRUGS COMPRISNG THE SAME - An anti-tumor polypeptide, having an amino acid sequence represented by FPGSDRF (SEQ ID NO. 15), X-FPGSDRF, FPGSDRF-Z, or X-FPGSDRF-Z, in which the various capital letters denote amino acids: F: phenylalanine; P: proline; G: glycine; S: serine; D: aspartic acid; R: arginine; S is a phosphorylated serine residue, X and Z are an amino acid residue or an amino acid sequence, respectively, X is one selected from the group consisting of F, (R) | 03-10-2016 |
20160113993 | THERAPEUTIC VITAMIN D CONJUGATES - The invention provides non-hormonal vitamin D conjugated to apelin proteins that result in increased absorption, bioavailability or circulating half-life when compared to non-conjugated forms. In some embodiments, the vitamin D targeting groups are coupled to the apelin proteins via the third carbon on the vitamin D backbone. | 04-28-2016 |
20160122383 | Peptide Ligation - The invention relates to a process for introducing a thiol group a to a carbonyl group in a side chain of a protected a-amino acid, said protected a-amino acid having protecting groups on both the α-amine group and the a-carboxyl group. The process comprises a) if the side chain contains a functional group comprising a heteroatom bearing a hydrogen atom, protecting said functional group; b) treating the protected amino acid with a base of sufficient strength to abstract a hydrogen atom a to the carbonyl group, so as to form an anion; c) treating the anion with a reagent of structure Pr-S-L in which L is a leaving group and Pr is a thiol-protecting group, so as to introduce a Pr-S- group a to the carbonyl group; and d) converting the Pr-S- group to an H-S-(thiol) group. This process may be used to prepare ligated peptides. | 05-05-2016 |
20160251398 | ANTIBACTERIAL ANTISENSE OLIGONUCLEOTIDE AND METHOD | 09-01-2016 |