Abstract
Antimicrobial proteins are a rich source of new lead compounds for the development of new drugs that will tackle global resistance towards existing antibiotics. Caenopore-5 (Cp-5) is an antimicrobial protein (AMP) expressed in the intestine of the nematode Caenorhabditis elegans and is a member of the lipid binding saposin-like-protein family, composed of 5 alpha-helices and 3 disulfide bonds. Substitution of the (7)Cys and (81)Cys by two selenocysteine U-7 and U-81 afforded a selenocysteine analogue [(7)Sec-(81)Sec]-Cp-5, which displayed a higher stability (using thermal circular dichroism) compared to the native protein Cp-5. [(7)Sec-(81)Sec]-Cp-5 and an N-terminal truncated peptide exhibited cell permeability similar to the wild type Cp-5.