Improved Antimicrobial Activity of Bovine Lactoferrin Peptide (LFcinB) Based on Rational Design

被引：5
作者：
Hong, Xiaokun [1 ]
Liu, Xueqian [1 ]
Su, Bingmei [1 ]
Lin, Juan [1 ]
机构：
[1] Fuzhou Univ, Coll Biol Sci & Engn, Fuzhou 350116, Fujian, Peoples R China
来源：
PROTEIN JOURNAL | 2023年 / 42卷 / 06期
基金：
中国国家自然科学基金;
关键词：
Bovine lactoferrin peptide; Actimicrobial activity; Rational design; Bioinformatics analysis; ANTIBACTERIAL ACTIVITY; MEMBRANE INTERACTIONS; ANTIBIOTIC-ACTIVITY; BIOLOGICAL-ACTIVITY; PROTEIN EXPRESSION; STABILITY; CHARGE; PURIFICATION; RESIDUES; AFFINITY;
D O I：
10.1007/s10930-023-10142-4
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Bovine lactoferrin peptide (LFcinB), as an antimicrobial peptide, is expected to be an alternative of antibiotics owing to its broad-spectrum antimicrobial activity and specific mechanism. However, the weak antimicrobial activity, high hemolysis, and poor stability of LFcinB limited its applications in the field of biomedicine, food and agriculture. In order to improve the antimicrobial activity of LFcinB, five mutants were designed rationally, of which mutant LF4 (M10W/P16R/A24L) showed highest antimicrobial activity. The bioinformatics analysis indicated that the improved antimicrobial activity of LF4 was related to its increased cations, higher amphiphilicity and the extension of the & beta;-sheet in the structure. These studies will highlight the important role of bioinformatic tools in designing ideal biopeptides and lay a foundation for further development of antimicrobial peptides.
引用
收藏
页码：633 / 644
页数：12
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