Investigation of the structure-activity relationship in ponericin L1 from Neoponera goeldii.

ABSTRACT: Naturally derived antimicrobial peptides have been an area of great interest because of high selectivity against bacterial targets over host cells and the limited development of bacterial resistance to these molecules throughout evolution. There are also a significant number of venom-derived peptides that exhibit antimicrobial activity in addition to activity against mammals or other organisms. Many venom peptides share the same net cationic, amphiphilic nature as host-defense peptides, making them an attractive target for development as potential antibacterial agents. The peptide ponericin L1 derived from Neoponera goeldii was used as a model to investigate the role of cationic residues and net charge on peptide activity. Using a combination of spectroscopic and microbiological app

SUBMITTER: Senetra AS 

PROVIDER: S-EPMC8086892 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature