Pós-Doc Gustavo Penteado Battesini Carretero

Gustavo Penteado Battesini Carretero

Biophysical and activity studies of antimicrobial peptide BP100 and a series of BP100 modified analogues

Antimicrobial peptides (AMPs) are a class of molecules present in a large variety of organisms that work as a primary defense against pathogenic microorganisms. BP100 (KKLFKKILKYL-NH2) is a short, highly cationic, synthetic AMP designed from melittin and Cecropin A, two known AMPs, that showed to be active against many bacteria and displayed low toxicity against human cells. BP100 have no defined structure in solution and acquired α-helical conformation upon interaction with model membranes; the membrane-bound form has an amphipathic character essential for its stabilization on the interface. In this project we evaluate the interaction of several BP100 analogues’ (Arg2-Arg5-BP100 and Arg-BP100), and analogs of BP100 alkylated on the C-terminal end (BP100- C16) of the peptides (Arg2-Arg5-BP100-C16 and Arg-BP100-C16) with membrane models using different physical techniques. The efficiency against bacteria and their possible toxic effect against human cell models will be determined.