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The effect of structural modification of antimicrobial peptides on their antimicrobial activity, hemolytic activity, and plasma stability
Author(s) -
Wang Taoran,
Zou Cunbin,
Wen Na,
Liu Xingdong,
Meng Zhao,
Feng Siliang,
Zheng Zhibing,
Meng Qingbin,
Wang Chenhong
Publication year - 2021
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.3306
Subject(s) - antimicrobial , peptide , hemolysis , chemistry , cysteine , antimicrobial peptides , amino acid , biochemistry , peptide sequence , cytotoxicity , combinatorial chemistry , in vitro , enzyme , biology , organic chemistry , gene , immunology
In this article, a series of modifications were made on an antimicrobial peptide F 2,5,12 W, 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.