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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.
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页码:7520 / 7529
页数:10
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