A New Structure-Activity Relationship of Linear Cationic α-helical Antimicrobial Peptides

Abstract

With the growing of pathogenic organisms’ resistibility to conventional antibiotics, antimicrobial peptides (AMPs), which have been isolated and characterized from tissues and organisms ranging from prokaryotes to humans, are recognized as a possible source of pharmaceuticals for the treatment of antibiotic-resistant bacterial infections. Many efforts have been made to increase the potency and specificity of these peptides so that they are toxic to microbes and not to mammals. A new structure-activity relationship of AMPs is revealed by analyzing the data of the antimicrobial assays here. Our results show that, not as in the receptor-mediated process, there is a linear correlation between the flexibility and the antimicrobial activity. The smaller the flexibility of the AMPs, the stronger the antimicrobial activity of the AMPs. This new structure-activity relationship may be used not only to predict the antimicrobial activity of AMPs from their sequences, but also in structural prediction, drug design and other AMPs’ researches.