The effect of structural modification of antimicrobial peptides on their antimicrobial activity, hemolytic activity, and plasma stability

JOURNAL OF PEPTIDE SCIENCE(2021)

引用 22|浏览10
暂无评分
摘要
In this article, a series of modifications were made on an antimicrobial peptide F2,5,12W, including altering the amino acid sequence, introducing cysteine and other typical amino acids, developing peptide dimers via disulfide bonds, and conjugating with mPEG, in order to enhance the antimicrobial activity, plasma stability, and reduce the hemolytic activity of peptides. The results showed that mPEG conjugation could significantly improve the plasma stability and reduce the hemolytic activity of peptides, while the antimicrobial activity decreased meanwhile. However, altering the sequence of the peptide without changing its amino acid composition had little impact on its antimicrobial activity and plasma stability. The introduction of cysteine enhanced the plasma stability of peptides conspicuously, but at the same time, the increased hydrophobicity of peptides increased their hemolysis. The antimicrobial mechanism and cytotoxicity of the peptides with relatively high antimicrobial activity were also studied. In general, this study provided some ideas for the rational design and structure optimization of antimicrobial peptides.
更多
查看译文
关键词
antimicrobial activity,antimicrobial peptide,hemolytic activity,plasma stability,structural modification
AI 理解论文
溯源树
样例
生成溯源树,研究论文发展脉络
Chat Paper
正在生成论文摘要