48 results about "Peptide backbone" patented technology
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Peptides and peptide backbone Any number of amino acids can chain together by successive peptide bonds. ... The alpha carbons from each amino acid alternate with the peptide bonds to form the “ backbone ” of the peptide. A similar linkage between a large number of amino acids forms polypeptides, which are called proteins when they are large enough and have a defined three-dimensional structure.
Peptide is disclosed which comprises D-enantiomers of amino acids and is capable of interacting with other β-strand structure to form β-sheet, wherein said peptide is selectively Nα-substituted in one edge (first) of the β-strand-forming section of said peptide while the other edge (second) in the opposite orientation to the first edge in view of peptide backbone plane remains Nα-unsubstituted. Such the Nα-substituted peptide is capable of preventing association of said peptide with other β-strand (target) but permits interaction of said peptide with target β-strand in separate peptide-containing molecules through the Nα-unsubstituted edge. The peptide is useful for preventing β-strand association or aggregation.
The invention discloses a pH-responsive non-helix-helix transition antibacterial polypeptide and a preparation method thereof. The method uses glutamic acid, an essential amino acid with biocompatibility, as a raw material, combined with the click chemistry method, to obtain a cationic polypeptide with a helical structure, which is prepared by modifying half of the maleic anhydride derivative through the side chain of the cationic polypeptide with a helical structure. The pH-responsive non-helical-helical transition antibacterial polypeptide has simple process, convenient operation and low cost, and can efficiently realize the secondary structure transformation under specific pH conditions, effectively reduce the biotoxicity of cationic polypeptides, and improve the bioavailability of cationic polypeptides Spend. In the present invention, through the modification of acid anhydrides with different pH responses, non-helical-helical transition antibacterial polypeptides with different pH conditions can be obtained, and the transformation from a low-activity non-helical structure to a high-activity helical structure can be realized under different physiological conditions. The conversion of cationic peptides can kill bacteria at the site of infection, which has broad application prospects.