Research Initiatives
Our laboratory operates at the intersection of structural biology and translational medicine focusing on variety of research frontiers. Explore our ongoing projects that are pushing the boundaries of science and medicine.

Artificial Intelligence based de novo cyclic antimicrobial peptide generation
Cyclic peptides offer proteolytic stability and membrane activity that linear antimicrobial peptides lack, yet no generative framework currently targets antimicrobial cyclic peptides. This works aims to develop and evaluate a deep generative model for de novo design of cyclic antimicrobial peptides.

Miniproteins
Miniproteins, defined as polypeptides comprising fewer than 100 amino acids, represent a unique and increasingly important class of biomolecules with remarkable structural diversity and functional versatility.

Protein Crystallography
The Protein Crystallography group in the Hazra Lab focuses on understanding the structural basis of β-lactamase-mediated antibiotic resistance.

Environmental Sampling and Modeling (include metagenomics and metabolomics)
The study includes microbiological analysis, advanced chromatography-based mass spectrometry, and metagenomics of all samples collected from 25 distinct geolocations across India.

Development of BL Testers For On-site detection of Drug Resistant Bacteria
Development of BL Testers for on-site detection of drug-resistant bacteria: BL-tester Basic, Environmental BL-Tester and, Advance BL tester.

MBL fold metallo hydrolase having β-lactam drug degrading activity
MBL-fold metallo-hydrolases are zinc-dependent enzymes characterized by a conserved αβ/βα sandwich structure known as the metallo-β-lactamase (MBL) fold. Among them, metallo-β-lactamases hydrolyze β-lactam antibiotics using one or two Zn²⁺ ions, rendering many clinically important drugs, including carbapenems, ineffective. Unlike serine β-lactamases, MBLs are not inhibited by classical β-lactamase inhibitors, making them a major challenge in antimicrobial therapy.

Global Beta-Lactamase Database (GBLD)
The Global Beta-Lactamase Database (GBLD) is a next-generation, integrative computational resource designed to transcend the limitations of sequence-centric repositories.

CTX-M Case Study
Extended-spectrum β-lactamases (ESBLs) have emerged as one of the most consequential antimicrobial resistance mechanisms of the 21st century. Among Class A β-lactamases which include TEM, SHV, CTX-M, VEB, and GES families CTX-M has risen to global dominance, with over 450 variants documented in the Beta-Lactamase Database (BLDB). The CTX-M designation reflects both its substrate profile (cefotaxime hydrolysis) and its geographic origin (Munich), where the first isolate was recovered from the ear of a 4-month-old child with otitis media. Over the last two decades, blaCTX-M-15 and blaCTX-M-14 have displaced other genotypes and become the predominant CTX-M alleles worldwide.

Escalating threat of antimicrobial resistance
The research addresses the escalating threat of antimicrobial resistance by investigating the structural and functional mechanisms of L1 and L2 beta-lactamases, particularly those produced by the opportunistic pathogen Stenotrophomonas maltophilia.

Structure and Function of Class-C β-lactamase
Protein purification, Circular Dichroism, Steady state Kinetic assay, Protein Modelling, Validation, Molecular Docking

Luciferase
Luciferase enzymes are oxidative enzymes and belong to the class of oxidoreductase enzymes, capable of decarboxylation and ATP hydrolysis. The emission of light is the result of a biochemical reaction in which substrates, i.e. luciferins, are oxidized by luciferase enzyme in presence of ATP, oxygen, and magnesium ions as cofactors.

Biomedical Samples
Our research primarily focuses on biomedical microorganisms isolated from clinically relevant samples, particularly from immunocompromised patients such as leukemia patients who are highly susceptible to opportunistic infections.

Dnazyme-HCR based AMR gene detection
A hybrid dual-mode biosensing device that combines HCR based DNAzymes and ATP-dependent bioluminescent quantification. The platform creates the folding-driven catalytic activation of metastable DNAzymes at the molecular level, where conformational rearrangement into catalytically competent structures is induced by target-specific recognition of resistance-associated DNA sequences.