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Cation–π Interactions in β-Lactamases: The Role in Structural Stability

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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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Abbreviations

PDB:

Protein data bank

CAPTURE:

Cation–π trends using realistic electrostatics

OPLS:

Optimized potentials for liquid simulations

Arg (R):

Arginine

Lys (K):

Lysine

Tyr (Y):

Tyrosine

Trp (W):

Tryptophan

Phe (F):

Phenylalanine

E es :

Electrostatic

E vdw :

van der Waals

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Acknowledgments

Dr. Anand Anbarasu gratefully acknowledges the Indian council of Medical Research (ICMR), Government of India Agency, for the research grant [IRIS ID: 2011-03260] to carry out this research. P. Lavanya thanks ICMR for the Research fellowship through the ICMR grant IRIS ID: 2011-03260. We would like to thank the management of VIT University for providing us the necessary facilities to carry out this research project.

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The authors declare there is no conflict of interest.

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Authors and Affiliations

  1. Medical and Biological Computing Laboratory, School of Biosciences and Technology, VIT University, Vellore, 632014, Tamil Nadu, India

    P. Lavanya, Sudha Ramaiah & Anand Anbarasu

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  1. P. Lavanya
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  2. Sudha Ramaiah
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  3. Anand Anbarasu
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Correspondence to Anand Anbarasu.

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Lavanya, P., Ramaiah, S. & Anbarasu, A. Cation–π Interactions in β-Lactamases: The Role in Structural Stability. Cell Biochem Biophys 66, 147–155 (2013). https://doi.org/10.1007/s12013-012-9463-x

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