30 results about "Α helical" patented technology

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.

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.

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.

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.

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.

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.

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.

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.

The present invention includes a novel class of highly specific protease inhibitors. In one embodiment, the inhibitors of the invention are α-helical in structure. In another embodiment, the present invention represents the first demonstration of a highly specific cysteine protease inhibitor.

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.

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.