Author

Tejavath Ajith

Indian Institute of Technology KharagpurORCID 0009-0008-7687-1204Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Microbiology· 2 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:bacteria (other)· 1 Assay:bulk RNA-seq· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

Anindya Sundar GhoshiD· 3 shared Bayomi BijuiD· 2 shared Diamond JainiD· 2 shared Ajit Ramesh Sawant· 1 shared Chiranjit ChowdhuryiD· 1 shared Debasmita ChatterjeeiD· 1 shared Jyoti Kumar VermaiD· 1 shared Piyali Datta Chakraborty· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersMicrobiology

Anindya Sundar GhoshORCID

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3 papers

Recent·Most cited

MicrobiologybioRxivPreprintJul 16, 2026

Placentrex disrupts the biofilm formation of Pseudomonas aeruginosa through multi-target transcriptional reprogramming.

Bayomi Biju, Ajit Ramesh Sawant, Sachin Maji…·Anindya Sundar Ghosh

This paper evaluates Placentrex's antibacterial and antibiofilm activity against Pseudomonas aeruginosa, identifying its mechanism involving multi-target transcriptional reprogramming.

DOI 10.64898/2026.05.22.727083

bacteria (other)bulk RNA-seq

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Molecular BiologybioRxivPreprintMay 23, 2026

Deciphering the role of the non-active site ancillary residues in maintaining the activity and substrate specificity of OXA-232 beta-lactamase

Tejavath Ajith, Bayomi Biju, Diamond Jain…·Anindya Sundar Ghosh

This study investigates the role of non-active site residues in OXA-232 beta-lactamase, showing their impact on activity, substrate specificity, and structural stability through site-directed mutagenesis and biophysical analysis.

DOI 10.64898/2026.05.22.727341

experimental assay

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MicrobiologyFEMS Microbiology LettersPeer-reviewedJan 1, 2025

Conserved ancillary residues situated proximally to the VIM-2 active site affect its metallo β-lactamase activity

Diamond Jain, Tejavath Ajith, Jyoti Kumar Verma…·Anindya Sundar Ghosh

The paper investigates the impact of specific amino acid substitutions near the VIM-2 active site on its metallo β-lactamase activity and stability, finding that N210A and D182A reduce catalytic efficiency and thermal stability.

1 citation

proteomicsexperimental assay

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