38 results about "HECT domain" patented technology

The invention relates to lipopeptide building blocks consisting of a peptide chain comprising a coiled-coil domain, linked covalently to a lipid moiety comprising long alkyl or alkenyl chains, and optionally linked to an antigen; and to helical lipopeptide bundles and synthetic virus-like particles formed by aggregation. The nanometer size and shape of these bundles and particles, their stability under aqueous physiological conditions, their chemical composition, the possibility to incorporate B- and T-cell epitopes, and their production by chemical synthesis, make them highly suitable as vaccine delivery vehicles.

A group of compounds that inhibit HIV replication by blocking HIV entry was identified. Two representative compounds, designated NB-2 and NB-64, inhibited HIV replication (p24 production) with IC₅₀ values <0.5 μg/ml. It was proved that NB-2 and NB-64 are HIV entry inhibitors by targeting the HIV gp41 since: 1) they inhibited HIV-mediated cell fusion; 2) they inhibited HIV replication only when they were added to the cells less than one hour after virus addition; 3) they did not block the gp120-CD4 binding; 4) they did not interact with the coreceptor CXCR4 since they failed to block anti-CXCR4 antibody binding to CXCR4-expressing cells; 5) they blocked the formation of the gp41 core that is detected by sandwich enzyme linked immunosorbent assay (ELISA) using a conformation-specific MAb NC-1; 6) they inhibited the formation of the gp41 six-helix bundle revealed by fluorescence native-polyacrylamide gel electrophoresis (FN-PAGE); and 7) they blocked binding of D-peptide to the hydrophobic cavity within gp41 coiled coil domain, modeled by peptide IQN17. These results suggested that NB-2 and NB-64 may interact with the hydrophobic cavity and block the formation of the fusion-active gp41 coiled coil domain, resulting in inhibition of HIV-1 mediated membrane fusion and virus entry.

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.

The invention is directed to functionalized self-assembling polypeptide nanoparticles, and to methods of using these nanoparticles to vaccinate against malaria. The functionalized SAPN comprises a self-assembling core, and at least one epitope fused to the self-assembling core. The self-assembling core comprises a pentameric coiled-coil domain, a trimeric coiled-coil domain, and a linker. The linker joins the pentameric coiled-coil domain and the trimeric coiled-coil domain. Particular sequences of the epitopes used in the vaccine are from the Plasmodium parasite.

Provided is an interparticle spacing material comprising a nucleic acid structure which comprises at least one nucleic acid lattice comprising a double helix domain; and at least one metal particle which is in contact with a plane of the nucleic acid lattice, in a direction extending obliquely or perpendicularly away from the plane; wherein the double helix domain comprises a hybridization area in which a single strand is hybridized with another single strand.

The present disclosure relates to recombinant or synthetic collagen-like proteins comprising at least one triple-helical domain and wherein the collagen-like protein is modified compared to a native bacterial collagen-like sequence.

The invention provides a two-color sea lavander herb gene LbHLH and application thereof. According to the invention, the full length of the gene LbHLH is obtained by performing cloning on a salt-secreting halophyte two-color sea lavander herb. The gene LbHLH comprises an open reading frame of 2067 bp, and is used for coding a protein consisting of 688 amino acids. The gene LbHLH has a typical helix-loop-helix (HLH) structural domain between amino acids 480-526. Experiments show that an arabidopsis thaliana plant for heterologous expression of the gene has the effects of promoting epidermal hair development, reducing root hair development and enhancing salt tolerance. A yeast two-hybrid experiment also shows that the gene LbHLH can interact with AtGL1, so that the gene LbHLH can play an important role in differentiation and salt resistance of hairy bodies and root hairs.

A biologically active complex comprising a peptide of up to 50 amino acids in length which comprises an alpha-helical domain of a protein which has membrane perturbing activity or a variant thereof which lacks cysteine residues, and oleic acid or a salt thereof, provided the protein is other than alpha-lactalbumin. Complexes of this type are useful in therapy, in particular cancer therapy.

The present invention relates to a fusion polypeptide comprising a carrier protein and a polypeptide of interest, the carrier protein has a plurality of helical domains linked by a loop, the polypeptide of interest is inserted into the loop of the carrier protein, the carrier protein obscuring a site of interest on the polypeptide of interest, therefore, the accessibility of the site is blocked. The invention also relates to polynucleotides and carriers encoding the fusion polypeptides, as well as host cells comprising the polynucleotides and/or carriers. Further, the invention also relates to application of the fusion polypeptide of the invention in the treatment of cancer and/or activation of immune cells.

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.