Hong Xiaokun, Liu Xueqian, Su Bingmei, Lin Juan
College of Biological Science and Engineering, Fuzhou University, Fuzhou, 350116, Fujian, China.
Protein J. 2023 Dec;42(6):633-644. doi: 10.1007/s10930-023-10142-4. Epub 2023 Aug 11.
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 β-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.
牛乳铁蛋白肽（LFcinB）作为一种抗菌肽，因其具有广谱抗菌活性和特定作用机制，有望成为抗生素的替代品。然而，LFcinB抗菌活性较弱、溶血率高且稳定性差，限制了其在生物医药、食品和农业领域的应用。为了提高LFcinB的抗菌活性，合理设计了5种突变体，其中突变体LF4（M10W/P16R/A24L）表现出最高的抗菌活性。生物信息学分析表明，LF4抗菌活性的提高与其阳离子增加、两亲性增强以及结构中β-折叠的延伸有关。这些研究将突出生物信息学工具在设计理想生物肽中的重要作用，并为抗菌肽的进一步开发奠定基础。
