Non-perfectly Amphipathic α-Helical Structure Containing the XXYXX Sequence Improves the Biological Activity of Bovine αs2-Casein Antimicrobial Peptides

被引:9
|
作者
Gu, Liya [1 ]
Sun, Changbao [1 ]
Chen, Lijun [2 ]
Pang, Shiyue [1 ]
Hussain, Muhammad Altaf [1 ]
Jiang, Chenggang [3 ]
Ma, Jiage [1 ]
Jiang, Zhanmei [1 ]
Hou, Juncai [1 ]
机构
[1] Northeast Agr Univ, Coll Food Sci, Key Lab Dairy Sci, Minist Educ, Harbin 150030, Heilongjiang, Peoples R China
[2] Beijing Sanyuan Foods Co Ltd, Natl Engn Res Ctr Dairy Maternal & Child Hlth, Beijing 100163, Peoples R China
[3] Chinese Acad Agr Sci CAAS, Harbin Vet Res Inst, Harbin 150001, Heilongjiang, Peoples R China
关键词
antimicrobial peptide; non-perfectly amphipathic; alpha-helical; mirror symmetrical; bactericidal mechanism; hemolysis; MEMBRANE INTERACTIONS; HYDROPHOBICITY; LACTOFERRICIN; LENGTH; SUBSTITUTION; SELECTIVITY; DESIGN; CELLS;
D O I
10.1021/acs.jafc.0c01377
中图分类号
S [农业科学];
学科分类号
09 ;
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.
引用
收藏
页码:7520 / 7529
页数:10
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