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Your search keyword '"Jiang, Chenggang"' showing total 6 results
Start Over Author "Jiang, Chenggang" Publisher american chemical society
6 results on '"Jiang, Chenggang"'

6. Non-perfectly Amphipathic α-Helical Structure Containing the XXYXX Sequence Improves the Biological Activity of Bovine α s2 -Casein Antimicrobial Peptides.

Author

Gu L, Sun C, Chen L, Pang S, Hussain MA, Jiang C, Ma J, Jiang Z, and Hou J

Subjects
Amino Acid Motifs, Amino Acid Sequence, Animals, Bacteria drug effects, Cattle, Microbial Sensitivity Tests, Protein Conformation, alpha-Helical, Caseins chemistry, Pore Forming Cytotoxic Proteins chemistry, Pore Forming Cytotoxic Proteins pharmacology
Abstract

Non-amphiphilic WIQPKTKVIPYVRYL (WI-6) derived from bovine α s2 -casein f (193-207) was modified by a defined mutation method to obtain five engineered peptides with mirror symmetry structures. The five engineered peptide sequences were WF-1 (WFQVKTRVRTKVQFW), FW-2 (FWRRYKKVKKYRRWF), FW-3 (FWQVIKKVKKIVQWF), FK-4 (FKQFYRRVRRYFQKF), and FR-5 (FRQWYRRVRRYWQRF). However, FW-2, FW-3, FK-4, and FR-5 had obvious XXYXX sequences. Among these, FW-3 was demonstrated to have the highest antibacterial activity, which indicates that the non-perfectly amphipathic α-helical structure containing the XXYXX sequence has a better bactericidal effect. Therefore, peptide FW-3 could be widely used as a substitute for antibiotics in food, medicine, and other fields. These findings provide a potential method for designing novel antimicrobial peptides.

Published
2020
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