期刊
CHEMICAL BIOLOGY & DRUG DESIGN
卷 94, 期 6, 页码 2051-2063出版社
WILEY
DOI: 10.1111/cbdd.13608
关键词
antimicrobial peptides; antimicrobial potency; bactericidal mechanism; tryptophan arrangement
资金
- National Natural Science Foundation of China [31872368, 31672434]
- China Agriculture Research System [CARS-35]
- Natural Science Foundation of Heilongjiang Province [TD2019C001]
- Weifang University Doctoral Foundation Program [2017BS10]
- Shandong Major Science and Technology Innovation Projects [2018CXGC0102]
It is traditionally believed that the distribution of tryptophan (Trp) residues is critical for the novo design of antimicrobial peptides (AMPs). However, there is scarce knowledge regarding Trp residues arrangement at the head group level. Thus, a set of alpha-helical AMPs containing different Trp residue arrangements at the N-/C-terminal of sequence were designed to increase the strategy database and analyze their biological activities. The arrangement of the N-terminal Trp residue significantly improved the bacteriostatic activity of the peptides, but the C-terminal Trp residue arrangement reduced the biocompatibility of them. WL and LW were effective against Gram-negative microbes and had high selectivity for bacteria as compared to human erythrocytes and mammalian cells. They both maintained a relatively desirable activity in the presence of physiological salts and serum. It is observed through electron microscope, flow cytometry and fluorescence spectroscopy that target peptides can penetrate bacterial cell membrane and kill it by damaging cell membrane integrity. Collectively, we determined the structure-activity relationship of Trp residue distributions in a symmetric sequence structure and filled the gap in knowledge related to Trp arrangements at the head group level. The obtained results will be helpful in designing of artificial peptide-based antimicrobials.
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