Lessons from a Single Amino Acid Substitution: Anticancer and Antibacterial Properties of Two Phospholipase A₂-Derived Peptides.

ABSTRACT: The membrane-active nature of phospholipase A₂-derived peptides makes them potential candidates for antineoplastic and antibacterial therapies. Two short 13-mer C-terminal fragments taken from snake venom Lys49-PLA₂ toxins (p-AppK and p-Acl), differing by a leucine/phenylalanine substitution, were synthesized and their bioactivity was evaluated. Their capacity to interfere with the survival of Gram-positive and Gram-negative bacteria as well as with solid and liquid tumors was assessed in vitro. Toxicity to red blood cells was investigated via in silico and in vitro techniques. The mode of action was mainly studied by molecular dynamics simulations and membrane permeabilization assays. Briefly, both peptides have dual activity, i.e., they act against both bacteria, in

SUBMITTER: Almeida JR 

PROVIDER: S-EPMC8929095 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature