Abstract
Aim: Group IIA bacteriocins, which contain unmodified amino acids and have antimicrobial activity, are a very broad group. Sakacins in this group are bacteriocins produced by Lactobacillus sakei. The most well-known sakacins are Sakacin A, G, K, P, and Q. In particular, Sakacin A and P are well characterized. This study aims to examine the interaction between a single monomer of PVA polymer and Sakacin P bacteriocin. Method: In t this study, the interaction of a single monomer of PVA polymer, which is among the water-soluble, biocompatible synthetic polymers, and Sakacin P bacteriocin, which has a protein structure, was investigated by molecular docking method. Results: As a result of our molecular docking study, the presence of binding affinity between the C2H4O monomer of PVA selected as the ligand and the Sakacin P protein selected as the receptor was determined. Conclusion: According to the results of the analysis, the presence of a strong inhibitor was detected between the ligand and the target. Therefore, this study can serve as a template for polymer-bacteriocin materials to be produced in the laboratory.
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