Design and Engineering of Antimicrobial Peptides Based on LPcin-YK3, an Antimicrobial Peptide Derivative from Bovine Milk.
We have previously derived a novel antimicrobial peptide, LPcin-YK3(YK3), based on lactophoricin and have successfully studied and reported on the relationship between its structure and function. In this study, antimicrobial peptides with improved antimicrobial activity, less cytotoxicity, and shorter length were devised and characterized on the basis of YK3, and named YK5, YK8, and YK11. The peptide design was based on a variety of knowledge, and a total of nine analog peptides consisted of one to three amino acid substitutions and C-terminal deletions. In detail, tryptophan substitution improved the membrane perturbation, lysine substitution increased the net charge, and excessive amphipathicity decreased. The analog peptides were examined for structural characteristics through spectroscopic analytical techniques, and antimicrobial susceptibility tests were used to confirm their activity and safety. We expect that these studies will provide a platform for systematic engineering of new antibiotic peptides and generate libraries of various antibiotic peptides.
['Kim|Ji-Sun|JS|', 'Jeong|Ji-Ho|JH|', 'Kim|Yongae|Y|']
D000595:Amino Acid Sequence D000818:Animals D000900:Anti-Bacterial Agents D023181:Antimicrobial Cationic Peptides D001419:Bacteria D016466:CHO Cells D002364:Caseins D002417:Cattle D002460:Cell Line D002470:Cell Survival D002522:Chlorocebus aethiops D003412:Cricetulus D052978:Disk Diffusion Antimicrobial Tests D020128:Inhibitory Concentration 50 D051379:Mice D008826:Microbial Sensitivity Tests D008892:Milk D008894:Milk Proteins D041681:NIH 3T3 Cells D010446:Peptide Fragments D017433:Protein Structure, Secondary D013329:Structure-Activity Relationship D014364:Tryptophan D014709:Vero Cells
Antimicrobial peptide lactophoricin tryptophan amphipathicity modification net positive charge