Insights into the Protein Binding of Short Cationic Antimicrobial Peptides

摘要

Cationic peptides (CAPs) derived from truncated lactoferricin are efficient antimicrobial substances [1]. Incorporation of bulky, hydrophobic synthetic amino acids creates compounds well suited for killing a range of Gram-positive bacteria with minimal inhibitory concentrations (MIC) down to ~1 μM for both antibiotic sensitive and methicillin resistant (MRSA) strains in in vitro studies [2]. However, pharmacokinetic factors like protein binding and proteolytic degradation (albeit their small size) of these compounds are issues that need be addressed and evaluated before they can be considered as more than "promising" candidates in the battle against resistant bacteria. This study was aimed at evaluating the extent and the effect of protein binding of this class of compounds. Binding of a range of promising CAPs to serum albumin and trypsin was studied through the use of calorimetry, molecular modeling and degradation studies [3,4].^