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48 results about "Peptide backbone" patented technology

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.

Compositions for the detection of enzyme activity in biological samples and methods of use thereof

The present invention provides for novel reagents whose fluorescence increases in the presence of particular proteases. The reagents comprise a characteristically folded peptide backbone each end of which is conjugated to a fluorophore. When the folded peptide is cleaved, as by digestion with a protease, the fluorophores provide a high intensity fluorescent signal at a visible wavelength. Because of their high fluorescence signal in the visible wavelengths, these protease indicators are particularly well suited for detection of protease activity in biological samples, in particular in frozen tissue sections. Thus this invention also provides for methods of detecting protease activity in situ in frozen sections.
Owner:ONCOIMMUNIN

Peptides containing N-substituted D-amino acids for preventing β-strand association

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.
Owner:SENEXIS LTD

Gene involved in synthesis of cyclic peptide compound, method for producing cyclic peptide compound using the same, and transformant comprising the same

This invention is intended to identify a gene cluster involved in biosynthesis of a cyclic peptide compound produced by a filamentous fungus of the Curvularia species and to establish a system for synthesizing such cyclic peptide compound. The gene is composed of a first module to a tenth module and encodes a protein having activity of synthesizing a nonribosomal peptide constituting a basic peptide backbone of a cyclic peptide compound produced by a filamentous fungus of the Curvularia species.
Owner:NAT INST OF ADVANCED IND SCI & TECH +2

A ph-responsive non-helix-helix transition antimicrobial polypeptide and preparation method thereof

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.
Owner:SOUTH CHINA UNIV OF TECH +1
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