Non-perfectly Amphipathic alpha-Helical Structure Containing the XXYXX Sequence Improves the Biological Activity of Bovine alpha(s2)-Casein Antimicrobial Peptides
文献类型： 外文期刊
第一作者： Gu, Liya
作者： Gu, Liya;Sun, Changbao;Pang, Shiyue;Hussain, Muhammad Altaf;Ma, Jiage;Jiang, Zhanmei;Hou, Juncai;Chen, Lijun;Jiang, Chenggang
作者机构：
关键词： antimicrobial peptide; non-perfectly amphipathic; alpha-helical; mirror symmetrical; bactericidal mechanism; hemolysis
期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）
ISSN： 0021-8561
年卷期： 2020 年 68 卷 28 期
页码：
收录情况： SCI
摘要： Non-amphiphilic WIQPKTKVIPYVRYL (WI-6) derived from bovine alpha(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 alpha-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.
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