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30 results about "Α helical" patented technology
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Stabilized compounds having secondary structure motifs
InactiveUS7192713B1Peptide-nucleic acidsGroup 8/9/10/18 element organic compoundsCrystallographyCarbon–carbon bond
The present invention provides novel stabilized crosslinked compounds having secondary structure motifs, libraries of these novel compounds, and methods for the synthesis of these compounds libraries thereof. The synthesis of these novel stabilized compounds involves (1) synthesizing a peptide from a selected number of natural or non-natural amino acids, wherein said peptide comprises at least two moieties capable of undergoing reaction to promote carbon-carbon bond formation; and (2) contacting said peptide with a reagent to generate at least one crosslinker and to effect stabilization of a secondary structure motif. The present invention, in a preferred embodiment, provides stabilized p53 donor helical peptides. Additionally, the present invention provides methods for disrupting the p53 / MDM2 binding interaction comprising (1) providing a crosslinked stabilized α-helical structure; and (2) contacting said crosslinked stabilized α-helical structure with MDM2.
Owner:PRESIDENT & FELLOWS OF HARVARD COLLEGE
Triazole macrocycle systems
InactiveUS7981999B2Simple structureExhibit biological activityPeptide-nucleic acidsTumor rejection antigen precursorsΑ helicalCombinatorial chemistry
The present invention provides novel peptidomimetic macrocycles and methods for their preparation and use, as well as amino acid analogs and macrocycle-forming linkers, and kits useful in their production. In various embodiments, the peptidomimetic macrocycles are of Formula I:The linker L includes a triazole moiety. Peptidomimetic macrocycles according to the invention may exhibit increased α-helical or beta sheet structure in aqueous solution compared to a corresponding non-macrocyclic polypeptide.
Owner:AILERON THERAPEUTICS INC
Peptide conjugates for the stabilization of membrane proteins and interactions with biological membranes
InactiveUS7087729B1Peptide-nucleic acidsCell receptors/surface-antigens/surface-determinantsΑ helicalAliphatic hydrocarbon
The present invention provides a novel class of detergents referred to herein as lipopeptide detergents. Lipopeptide detergents comprise an amphipathic α-helical peptide having a hydrophobic or neutral face and a hydrophilic face. To each end of this peptide is covalently linked an aliphatic hydrocarbon tail, these aliphatic tails being linked thereto such that they associate with the hydrophobic or neutral face of the peptide. Lipopeptide detergents can advantageously be used to stabilize membrane proteins in the absence of a phospholipid bilayer in a manner that preserves the native conformation and permits the subsequent crystallization thereof.
Owner:UNIV HEALTH NETWORK
Stabilized bioactive peptides and methods of identification, synthesis, and use
InactiveUS20060099571A1Slow down rate of intracellular degradationBacteriaPeptide/protein ingredientsLac operonΑ helical
An intracellular selection system allows screening for peptide bioactivity and stability. Randomized recombinant peptides are screened for bioactivity in a tightly regulated expression system, preferably derived from the wild-type lac operon. Bioactive peptides thus identified are inherently protease- and peptidase-resistant. Also provided are bioactive peptides stabilized by a stabilizing group at the N-terminus, the C-terminus, or both. The stabilizing group can be a small stable protein, such as the Rop protein, glutathione sulfotransferase, thioredoxin, maltose binding protein, or glutathione reductase, an α-helical moiety, or one or more proline residues.
Owner:PEPTIDE BIOSCI
Fabrication of a cartilage implant
InactiveUS6852331B2Efficient manufacturingSure easyBiocideBone implantΑ helicalMesenchymal stem cell
A method of fabricating a cartilage implant including embedding and growing chondrocytes or mesenchymal stem cells in a three-dimensional substrate. The substrate contains randomly rewound α-helical monomers of type I collagen.
Owner:TAIPEI BIOTECH
Selective detection of proteins that contain two or more alpha-helical transmembrane domains
Embodiments of the present invention provide a staining solution and of method of using the staining solution for selectively detecting proteins that contain two or more α-helical transmembrane domains. The staining solution comprises a lipophilic dyes and at least about a 30% hydrophobic solvent. The dyes of the present are represented by the general formula A-B-E wherein A is a nitrogen heterocycle, B is a bridge moiety and E is an electron pair accepting moiety that comprises either a carbonyl or nitrogen atom. In one embodiment these lipophilic dyes are merocyanine dye, a cyanine dye, a styryl dye or a carbazolylvinyl dye.
Owner:LIFE TECH CORP
Stabilized bioactive peptides and methods of identification, synthesis, and use
InactiveUS7365162B2Slow down rate of intracellular degradationBacteriaPeptide/protein ingredientsLac operonWild type
An intracellular selection system allows screening for peptide bioactivity and stability. Randomized recombinant peptides are screened for bioactivity in a tightly regulated expression system, preferably derived from the wild-type lac operon. Bioactive peptides thus identified are inherently protease- and peptidase-resistant. Also provided are bioactive peptides stabilized by a stabilizing group at the N-terminus, the C-terminus, or both. The stabilizing group can be a small stable protein, such as the Rop protein, glutathione sulfotransferase, thioredoxin, maltose binding protein, or glutathione reductase, an α-helical moiety, or one or more proline residues.
Owner:PEPTIDE BIOSCI
Multi-domain amphipathic helical peptides and methods of their use
Disclosed herein are peptides or peptide analogs with multiple amphipathic α-helical domains that promote lipid efflux from cells via an ABCA1-dependent pathway. Also provided herein are methods of using multi-domain amphipathic α-helical peptides or peptide analogs to treat or inhibit dyslipidemic disorders. Methods for identifying non-cytotoxic peptides that promote ABCA1-dependent lipid efflux from cells are also disclosed herein.
Owner:UNITED STATES OF AMERICA
Targeted human-interferon fusion proteins
ActiveUS9492562B2Low affinityDecrease of bioactivityPeptide/protein ingredientsAntibody mimetics/scaffoldsLow affinityDisease
This disclosure relates to a modified α-helical bundle cytokine, with reduced activity via an α-helical bundle cytokine receptor, wherein the α-helical bundle cytokine is specifically delivered to target cells. Preferably, the α-helical bundle cytokine is a mutant, more preferably it is a mutant interferon, with low affinity to the interferon receptor, wherein the mutant interferon is specifically delivered to target cells. The targeting is realized by fusion of the modified α-helical bundle cytokine to a targeting moiety, preferably an antibody. This disclosure relates further to the use of such targeted modified α-helical bundle cytokine to treat diseases. A preferred embodiment is the use of a targeted mutant interferon, to treat diseases, preferably viral diseases and tumors.
Owner:VLAAMS INTERUNIVERSITAIR INST VOOR BIOTECHNOLOGIE VZW +4
Core structure of gp41 from the HIV envelope glycoprotein
Described are the crystal structure of the α-helical domain of the gp41 component of HIV-1 envelope glycoprotein which represents the core of fusion-active gp41, methods of identifying and designing drugs which inhibit gp41 function and drugs which do so.
Owner:WHITEHEAD INST FOR BIOMEDICAL RES
Multi-domain amphipathic helical peptides and methods of their use
Owner:UNITED STATES OF AMERICA
Antimicrobial kinocidin compositions and methods of use
The present invention provides novel kinocidin peptides comprising a C-terminal portion of a kinocidin, wherein the C-terminal portion encompasses an α-helical secondary structure and further displays antimicrobial activity. The kinocidin peptides of the invention are derived from and correspond to a C-terminal portion of a kinocidin that includes a γKC core and that can be a CXC, CC, or C class chemokine. Structural, physicochemical and functional properties of this novel class of antimicrobial peptides and amino acid sequences of particular kinocidin peptides are also disclosed. The invention also provides related antimicrobial methods.
Owner:LOS ANGELES BIOMEDICAL RES INST AT HARBOR UCLA MEDICAL CENT
Peptides promoting lipid efflux via abca1 and activating a lipoprotein lipase
ActiveUS20110033518A1Promote lipid effluxImprove lipophilicityOrganic active ingredientsApolipeptidesDiseaseA lipoprotein
Disclosed herein are peptides and peptide analogs with multiple amphipathic α-helical domains that promote lipid efflux from cells via an ABCA1-dependent pathway, as well as peptides that activate lipoprotein lipase, and compositions comprising such peptides or combinations thereof. Also provided herein are methods of using multi-domain amphipathic α-helical peptides or peptide analogs to treat or inhibit dyslipidemic disorders. Methods for identifying non-cytotoxic peptides that promote ABCA1-dependent lipid efflux from cells and activate lipoprotein lipase within cells are also disclosed herein.
Owner:UNITED STATES OF AMERICA
A dual-targeted therapeutic peptide for nasopharyngeal carcinoma, nanoparticles carrying same and uses thereof
ActiveUS20150344525A1Growth inhibitionSmall sizeUltrasonic/sonic/infrasonic diagnosticsPowder deliveryMedicineNanoparticle
Disclosed is a dual-targeted therapeutic peptide for nasopharyngeal carcinoma formed by covalently linking a targeted therapeutic peptide for nasopharyngeal carcinoma, a peptide linker and a targeted therapeutic peptide with an α-helical structure for nasopharyngeal carcinoma. Also disclosed is a nanoparticle containing the peptide. The peptide and the nanoparticle can be used to treat nasopharyngeal carcinoma.
Owner:HUAZHONG UNIV OF SCI & TECH
Alpha-helical protein based materials and methods for making same
InactiveUS20050034280A1Monocomponent protein artificial filamentPeptide/protein ingredientsFiberΑ helical
The invention relates to a method of producing useful materials from filament-forming α-helical proteins or filaments made of such proteins. The method comprises allowing filament-formingα-helical proteins to self-assemble into α-helix containing filaments and forming fibres, films or bulk materials from the filaments. The materials are stretched to strain the filaments so that the α-helices substantially irreversibly change to β-sheet forms. The filament-forming α-helical proteins can comprise intermediate filament proteins. In a specific embodiment, the filament-forming proteins comprise hagfish slime thread IF proteins.
Owner:GOSLINE JOHN M DR +2
Peptides promoting lipid efflux
Disclosed herein are peptides and peptide analogs with multiple amphipathic α-helical domains that promote lipid efflux from cells via an ABCA1-dependent pathway, as well as peptides that activate lipoprotein lipase, and compositions comprising such peptides or combinations thereof. Also provided herein are methods of using multi-domain amphipathic α-helical peptides or peptide analogs to treat or inhibit dyslipidemic disorders. Methods for identifying non-cytotoxic peptides that promote ABCA1-dependent lipid efflux from cells and activate lipoprotein lipase within cells are also disclosed herein.
Owner:UNITED STATES OF AMERICA
Bilaterally-substituted tricyclic compounds for the treatment of human immunodeficiency virus type-1 (hiv-1) infection and other diseases
InactiveUS20160108024A1Inhibiting RRE-Rev interactionDull appearanceAntibacterial agentsBiocideDiseaseΑ helical
The invention relates to novel bilaterally-substituted tricyclic compounds and pharmaceutical compositions containing them, for use as medicaments.Due to their ability to interact with an internal RNA loop and to mimic a protein α-helix these compounds are effective in the treatment and / or prevention of HIV-1 (Human Immunodeficiency Virus-1) infection and other diseases such as those caused by other RNA viruses and by gram-positive and gram-negative bacteria, or infectious or chronic diseases responsive to inhibition of DNA transcription, or infectious or chronic diseases where these compounds can be used to modulate the function of RNA internal loops, or infectious or chronic diseases where these compounds can be used as agonists or inhibitors of α-helical proteins in interaction with other biomolecules.
Owner:INST DE SALUD CARLOS III +2
Novel Alpha-Helical Peptidomimetic Inhibitors And Methods Using Same
Owner:THE TRUSTEES OF THE UNIV OF PENNSYLVANIA
Nociceptin mimetics
InactiveUS8921306B2Negligible alpha helical structureIncrease serum stabilityNervous disorderImmunoglobulinsDiseaseΜ-opioid receptor
The present invention relates to nociceptin peptide mimetics that have α-helical structures and bind to and modulate the opioid receptor-like-1 (ORL-1) receptor. The peptide mimetics are constrained cyclic nociceptin analogs which have either agonist or antagonist activity. Pharmaceutical compositions comprising the nociceptin peptide mimetics and methods of treating or preventing a disease or condition ameliorated by modulating the ORL-1 receptor are also described.
Owner:THE UNIV OF QUEENSLAND
Nanoemulsions
ActiveUS20150132395A1Improved pharmacokinetic and targeting propertyEasy to prepareBiocidePeptide/protein ingredientsActive agentΑ helical
The invention relates to nanoemulsions useful for analytical techniques and delivery of cargoes such as pharmaceutically active agents. In particular, the invention relates to nanoemulsions comprising an oil phase dispersed in an aqueous phase and at least two peptide surfactants adsorbed at the liquid-liquid interface, one peptide surfactant comprising a short peptide sequence having α-helical propensity and at least one second polypeptide surfactant comprising at least two peptide sequences having α-helical propensity linked by a linking sequence of 3 to 11 amino acid residues. Optionally the at least one second polypeptide surfactant comprises at least one pharmacokinetic modifying agent and / or a targeting agent. Furthermore, the nanoemulsion may further comprise a cargo such as a pharmaceutically active agent.
Owner:THE UNIV OF QUEENSLAND
Nociceptin mimetics
InactiveUS20130157928A1Negligible alpha helical structureIncrease serum stabilityNervous disorderImmunoglobulinsDiseasePeptide mimetic
The present invention relates to nociceptin peptide mimetics that have α-helical structures and bind to and modulate the opioid receptor-like-1 (ORL-1) receptor. The peptide mimetics are constrained cyclic nociceptin analogues which have either agonist or antagonist activity. Pharmaceutical compositions comprising the nociceptin peptide mimetics and methods of treating or preventing a disease or condition ameliorated by modulating the ORL-1 receptor are also described.
Owner:THE UNIV OF QUEENSLAND
Nanoemulsions
ActiveUS9554995B2Improved pharmacokinetic and targeting propertyEasy to preparePeptide-nucleic acidsPeptide/protein ingredientsActive agentΑ helical
The invention relates to nanoemulsions useful for analytical techniques and delivery of cargoes such as pharmaceutically active agents. In particular, the invention relates to nanoemulsions comprising an oil phase dispersed in an aqueous phase and at least two peptide surfactants adsorbed at the liquid-liquid interface, one peptide surfactant comprising a short peptide sequence having α-helical propensity and at least one second polypeptide surfactant comprising at least two peptide sequences having α-helical propensity linked by a linking sequence of 3 to 11 amino acid residues. Optionally the at least one second polypeptide surfactant comprises at least one pharmacokinetic modifying agent and / or a targeting agent. Furthermore, the nanoemulsion may further comprise a cargo such as a pharmaceutically active agent.
Owner:THE UNIV OF QUEENSLAND
Optimized polypeptide for a subunit vaccine against avian reovirus
An isolated polypeptide comprising an amino acid sequence corresponding to the amino acid residues forming a full or partial α-helical domain, the hinge domain, the β-triple spiral domain and a full or partial globular head domain of an avian reovirus sigma C protein, and lacking the amino acid sequence that is N-terminal to said α-helical domain is provided. Furthermore, a vaccine comprising, or a viral vector expressing, at least one of the isolated polypeptides of the present invention is provided.
Owner:GAVISH GALILEE BIO APPL
Dual-targeted therapeutic peptide for nasopharyngeal carcinoma, nanoparticles carrying same and uses thereof
ActiveUS9371364B2Growth inhibitionSmall sizePowder deliveryTumor rejection antigen precursorsMedicineNanoparticle
Disclosed is a dual-targeted therapeutic peptide for nasopharyngeal carcinoma formed by covalently linking a targeted therapeutic peptide for nasopharyngeal carcinoma, a peptide linker and a targeted therapeutic peptide with an α-helical structure for nasopharyngeal carcinoma. Also disclosed is a nanoparticle containing the peptide. The peptide and the nanoparticle can be used to treat nasopharyngeal carcinoma.
Owner:HUAZHONG UNIV OF SCI & TECH
Reovirus vaccines and methods of use therefor
The present invention provides for modified reoviruses that carry α-helical epitopes from a variety of pathogens, as well as methods of using such modified reoviruses to generate immune responses against those epitopes in hosts.
Owner:VANDERBILT UNIV
Alpha-helical peptidomimetic inhibitors and methods using same
ActiveUS9670250B2Electrically conductive connectionsCells structural combinationΑ helicalCysteine Proteinase Inhibitors
Owner:THE TRUSTEES OF THE UNIV OF PENNSYLVANIA
Bilaterally-substituted tricyclic compounds for the treatment of human immunodeficiency virus type-1 (HIV-1) infection and other diseases
InactiveUS9586943B2Avoid interactionDull appearanceAntibacterial agentsOrganic compound preparationDiseaseΑ helical
Owner:INST DE SALUD CARLOS III +2
Designed biosurfactants, their manufacture, purification and use
InactiveUS20150031600A1Low technical requirementsLimited foam stabilityBiocideOrganic detergent compounding agentsStimuli responsiveΑ helical
The present invention relates to designed polypeptide biosurfactants that may be prepared by recombinant technology in commercially useful amounts and purified by simple non-chromatographic methods. The designed polypeptide biosurfactants comprise at least one stimuli-responsive amino acid residue or at least one glutamine or asparagine residue and may be useful in modulating the stability of a foam, alone or in combination with an α-helical peptide. The designed polypeptide biosurfactant may be useful in the formation and collapse of foams in foods, beverages, pharmaceuticals, personal care products, cosmetics, cleaning products, mineral recovery, bioremediation, oil recovery and laundry products. The designed biosurfactants may also be useful in recombinant production and purification of peptides, polypeptides and proteins.
Owner:THE UNIV OF QUEENSLAND
Antimicrobial alpha-helical cationic polypeptides
ActiveUS20180179336A1High antibacterial activityImprove breathabilityAntibacterial agentsBiocideProteinase activitySide chain
The invention provides antimicrobial polypeptides (AMPs) with high radial amphiphilicity. Unlike typical AMPs characterized by facial amphiphilicity or biomimetic antimicrobial polymers with randomly distributed charged and hydrophobic groups, these new AMPs are homo-polypeptides with radially amphiphilic structure. They adopt a stable α-helical conformation with a hydrophobic helical core and a charged exterior shell, formed by flexible hydrophobic side chains with terminal charge group. The radially amphiphilic polypeptides offer several advantages over conventional AMPs with regard to stability against protease and simplicity of design. They also exhibit high antibacterial activity against both Gram-negative and Gram-positive bacteria and low hemolytic activity. The AMPs thus provide a general platform for treating drug-resistant bacterial infections.
Owner:THE BOARD OF TRUSTEES OF THE UNIV OF ILLINOIS
Selective Detection of Proteins that Contain Two or More Alpha-Helical Transmembrane Domains
InactiveUS20100267078A1Microbiological testing/measurementPeptide preparation methodsStainingNitrogen
Owner:LIFE TECH CORP
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