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OJBTM

Online Journal of Bioinformatics

Volume 22 (3): 153-168, 2021.


Homology docking SHV β-lactamases for drug resistance.

 

Mohd Hassan Baig, Shazi Shakil and Asad U Khan.

 

Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India

 

ABSTRACT

 

Baig MH, Shakil S, Khan AU., Homology docking SHV β-lactamases for drug resistance, Onl J Bioinform., 22 (3): 153-168, 2021. Extended-spectrum-β-lactamases (ESBLs) in bacteria impart resistance to cephalosporins. SHV enzymes in ESBLs and binding of SHV-48, SHV-61, SHV-89, SHV-95 or SHV-105 to β-lactamase inhibitors has not been reported. We generated homology 3D model structure of SHV enzymes validated for stereo chemical properties. We targeted active site amino acid residues of SHV enzyme model to predict binding of inhibitors by energy docking. All SHV variants except SHV-61 interacted with clavulanic acid through S70, S130, K234 and A237, as residues. Of 20 docking interactions S70 and A237 were crucial for correct positioning of inhibitors on binding sites in 12 and 14 instances, respectively. By energy and Ki calculations, Penem1 was most efficient inhibitor against all bacterial enzymes, excluding SHV-105, where LN1-255 was most efficient.

 

Key Words: SHV β-lactamases, Homology, Docking, 3D model, Drug resistance.


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