Abstract

Background: β-lactamase is an enzyme that plays a role in the occurrence of antibiotic resistance against Methicillin-resistant Staphylococcus aureus (MRSA) bacteria. Viscosin is a lipopeptide biosurfactant produced by the Pseudomonas group bacteria. A study states that Viscosin has strong antibacterial properties.Aims: This study aims to determine the interactions that occur with Viscosin and β-lactamase enzymes.Methods: Researchers used the in-silico method to determine the molecular interactions that occurred computationally. The protein used was β-lactamase protein obtained from the Protein Data Bank and Viscosin ligand obtained from the PubChem web server, and we used native ligands as control. Pharma expert web server and Pyrx, Pymol, and Discovery Studio software were used in this research.Results: The results showed that Viscosin has high activity as an antibiotic and is predicted to be a membrane integrity antagonist. The binding affinity interaction that occurs between Viscosin-β-lactamase is -7.3 kcal/mol. The affinity is lower than the control.Conclusion: Viscosin was predicted to have strong antibacterial properties, but the binding interaction was lower than the control. However, exploration of Viscosin compounds and further research to determine the antibacterial effect of Viscosin against MRSA and other bacteria is needed to against antibiotic resistance.

Highlights

  • Methicillin-resistant Staphylococcus which is the β-lactamase enzyme, which has a aureus (MRSA) is a pathogenic strain of low affinity for β-lactam antibiotics.[1]

  • The results showed that Viscosin has high activity as an antibiotic and is predicted to be a membrane integrity antagonist

  • This lipopeptide is produced by the bacteria Pseudomonas fluorescens.[4,5,6,7] In previous studies, Pseudomonas fluorescens membrane extracts' ability to have an antibacterial activity that can destroy the integrity of tuberculosis cell membranes.[5,8]

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Summary

INTRODUCTION

Methicillin-resistant Staphylococcus which is the β-lactamase enzyme, which has a aureus (MRSA) is a pathogenic strain of low affinity for β-lactam antibiotics.[1]. A study states that this lipopeptide has antibacterial, antifungal properties against the fungus Aspergillus fumigatus. This lipopeptide is produced by the bacteria Pseudomonas fluorescens.[4,5,6,7] In previous studies, Pseudomonas fluorescens membrane extracts' ability to have an antibacterial activity that can destroy the integrity of tuberculosis cell membranes.[5,8]. Simulation of drug design interactions using silicone can predict an interaction mechanism between the ligand and target protein and the bond energy.(9 This study will predict the molecular interaction mechanism between Viscosin as an antibiotic candidate against MRSA using in-silico approach

Study Design
CONCLUSION
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