Designing Analogs of SAAP-148 with Enhanced Antimicrobial and Anti-LPS Activities.

ABSTRACT: SAAP-148, a derivative of LL-37, exhibits a well-defined amphipathic structure and enhanced antimicrobial activity; however, it also displays significant cytotoxicity towards human cells. In this study, we employed Lys-scan to produce a series of amphiphilic SAAP-148 analogs derived from the SAAP-148 sequence to investigate the impact of the distribution of positively charged residues on the biological viability of the antimicrobial peptides (AMPs). The physical properties and biological activity of the designed peptides were subsequently compared. The substitution of lysine resulted in an increase in the overall charge of SAAP-148 and a decrease in its overall hydrophobicity and hyd. moment, except for SAAP-10 where an analogue substitution occurred at the 18th residue. The replacement of

SUBMITTER: Gan L 

PROVIDER: S-EPMC11546786 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature