Cation-π interactions in β-lactamases: the role in structural stability
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Updated: May 17, 2026

The Use of a β-lactamase-based Conductimetric Biosensor Assay to Detect Biomolecular Interactions
Published on: February 1, 2018
P Lavanya1, Sudha Ramaiah, Anand Anbarasu
1Medical and Biological Computing Laboratory, School of Biosciences and Technology, VIT University, Vellore, 632014, Tamil Nadu, India.
Abstract:
β-lactam group of antibiotics is the most widely used therapeutic molecules for treating bacterial infections. The main mode of bacterial resistance to β-lactams is by β-lactamases. In the present study, we report our results on the role of cation-π interactions in β-lactamases and their environmental preferences. The number of interactions formed by arginine is higher than lysine in the cationic group, while tyrosine is comparatively higher than phenylalanine and tryptophan in the π group. Our results indicate that cation-π interactions might play an important role in the global conformational stability of β-lactamases.
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