MOLECULAR MODELING OF CRUZIOSEPTIN CC-16 EXTRACTED FROM THE FROG Cruziohyla calcarifer
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Abstract
The increasing development of resistance to antibiotics by the microbial world is a growing problem and in response new molecules with antimicrobial potential are being studied, among them antimicrobial peptides such as Cruzioseptins. This work presents a preliminary computational study of Cruzioseptin CC-16 extracted from exudate from the skin of the frog Cruziohyla calcarifer. Based on the amino acid sequence of the peptide, different computational studies were carried out, including the prediction of its physicochemical properties and its secondary structure. In addition to this, a molecular docking study of Cruzioseptin CC-16 was carried out with different enzymes of biological importance for microorganisms such as Escherichia coli, Staphylococcus aureus and Candida albicans, and with molecules present in the bacterial cell membrane. The results showed that Cruzioseptin CC-16 is a 23 residues long peptide with a predominant alpha helical conformation, an isoelectric point of 10.73, a basic charge of +3 and a net charge at pH 7 of +3.1, in addition of having more than 50 % of its structure made up of hydrophobic amino acids, fitting the definition of a cationic antimicrobial peptide. Preliminary molecular docking studies show that a mechanism of action based on enzyme inhibition is not possible mainly due to the size of the peptide, while a mechanism based on a concentrated attack on the microbial membrane may be viable due to the electrostatic interactions of the Cruizoseptin CC-16 with different components of the membrane.
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