Resumen:
A computational study of the peptides Cruzioseptin-4 and Pictuseptin-1, identifed in Cruziohyla
calcarifer and Boana picturata respectively, has been carried out. The studies on Cruzioseptin-4 show
that it is a cationic peptide with a chain of 23 amino acids that possess 52.17% of hydrophobic amino
acids and a charge of+ 1.2 at pH 7. Similarly, Pictuseptin-1 is a 22 amino acids peptide with a charge
of + 3 at pH 7 and 45.45% of hydrophobic amino acids. Furthermore, the predominant secondary
structure for both peptides is alpha-helical. The physicochemical properties were predicted using
PepCalc and Bio-Synthesis; secondary structures using Jpred4 and PredictProtein; while molecular
docking was performed using Autodock Vina. Geometry optimization of the peptides was done using
the ONIOM hybrid method with the HF/6-31G basis set implemented in the Gaussian 09 program.
Finally, the molecular docking study indicates that the viable mechanism of action for both peptides
is through a targeted attack on the cell membrane of pathogens via electrostatic interactions with
diferent membrane components, leading to cell lysis.
