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Prof. Sharmistha Sinha

Professor, Scientist-F

Sinha Lab: Cracking the Code of Biomolecular Self-Assembly: The Sinha Lab is on a mission to decode biomolecular self-assembly—the invisible architect of life. We work at the intersection of biophysics, phase separation, genetic engineering, and disease biology, tackling self-assembly from three dynamic angles: Natural Compartmentalization – How do cells build molecular ‘tiny homes’? We study bacterial microcompartments (BMCs) as model organelles to uncover the physics of phase separation and protein interactions. Synthetic Biology – Can we hijack nature’s self-assembly tricks? We engineer smart nanoreactors and biomaterials by repurposing microbial compartments for catalysis, bioenergy, and targeted drug delivery. Disease Biology – When self-assembly goes rogue. From Salmonella’s virulence strategies to misfolded protein aggregates in neurodegeneration, we investigate how phase separation fuels pathogenesis—and how to stop it. By blending cutting-edge microscopy, modeling, and genetic rewiring, we push the boundaries of self-assembly research. If you love molecular puzzles and want to design the future of biology, join us! Do write to us at sinhas@inst.ac.in for more info.

Contact Information :

  • Sinha Lab: Engineering Order in Molecular Chaos

    At Sinha Lab, we chase the molecular logic behind biomolecular self-assembly—the force that builds life and, when misregulated, fuels disease. We explore natural compartmentalization through bacterial microcompartments (BMCs), using them as blueprints to understand organelle biogenesis. We rewire these principles in synthetic biology, engineering smart nanofactories for catalysis, biomaterials, and targeted drug delivery. On the disease front, we dissect how liquid–liquid phase separation (LLPS) drives pathogenicity in Salmonella and protein aggregation in neurodegeneration. With a toolkit spanning biophysics, genetic engineering, and advanced imaging, we turn molecular self-assembly into both a playground and a battleground—revealing its rules and bending them to our will. 

  • Molecular Legos of Life & Disease

    Cracking the molecular code of liquid–liquid phase separation (LLPS) to understand how cells build compartments—and how misfolded proteins hijack these mechanisms in neurodegeneration, cancer, and bacterial pathogenesis.

  • Hijacking Bacterial Nano-Factories 

    Repurposing bacterial microcompartments (BMCs) as modular synthetic reactors, tuning their protein shells, enzyme loading, and genetic circuits for applications in catalysis, metabolic engineering, and antimicrobial strategies.

  • Molecular Chaos into Controlled Chemistry 

    Using phase separation to create barrier-free catalytic zones, confining protein–metal nanocomposites to supercharge enzymatic activity, with game-changing implications for synthetic biology and bio-inspired materials.

Current Group Members

  • ISHANI SHARMA

    ISHANI SHARMA

    Email: ishani.ph23228@inst.ac.in

    Reg. No.: PH23228

  • MR. S M ROSE

    MR. S M ROSE

    Email: smrose.ph21234@inst.ac.in

    Reg. No.: PH21234

  • MS. AARCHA RADHAKRISHNAN

    MS. AARCHA RADHAKRISHNAN

    Email: aarcha.ph21202@inst.ac.in

    Reg. No.: PH21202

  • MS. PREETI NEGI

    MS. PREETI NEGI

    Email: preeti.ph20209@inst.ac.in

    Reg. No.: PH20209

  • MS. DIMPLE GOEL

    MS. DIMPLE GOEL

    Email: dimple.ph20210@inst.ac.in

    Reg. No.: PH20210

  • MS.SIMERPREET KAUR

    MS.SIMERPREET KAUR

    Email: simerpreet.ph17224@inst.ac.in

    Reg. No.: PH17224

  • MS. HARPREET KAUR

    MS. HARPREET KAUR

    Email: harpreet.ph19201@inst.ac.in

    Reg. No.: PH19201

  • MS. SILKY

    MS. SILKY

    Email: silky.ph19202@inst.ac.in

    Reg. No.: PH19202

Alumni

  • BHAVIKA ARORA

    BHAVIKA ARORA

    Reg. No.: IN-2024/05

    Designation: Intern Student

    Jan 2024 - Jun 2024

  • MR. GAURAV KUMAR

    MR. GAURAV KUMAR

    Reg. No.: Ph17202

    Designation: PhD Scholar

    Aug 2017 - Feb 2023

  • MS. ANKUSH GARG

    MS. ANKUSH GARG

    Reg. No.: PH15206

    Designation: PhD Scholar

    Aug 2015 - Dec 2021

  • MR. NAIMAT KALIM BARI

    MR. NAIMAT KALIM BARI

    Reg. No.: PH14210

    Designation: PhD Scholar

    Aug 2014 - Jul 2020

  • 1.

    Protein-protein interactions as determinants of operon architecture , Silky Bedi , S.M. Rose , Simerpreet Kaur 1 , Preeti Negi 1 , Sharmistha Sinha , BBA Gen Subjects , just accepted , just accepted , just accepted , https://doi.org/10.1016/j.bbagen.2025.130794
  • 2.

    Bile Acids as Modulators of α-Synuclein Aggregation: Implications for Parkinson’s Therapy , H Kaur, D Swadia, S Sinha , ACS Chemical Neuroscience , 2024 , 15 (21), , 4055-4065 , https://doi.org/10.1021/acschemneuro.4c00459
  • 3.

    Substrate-induced phase transition within liquid condensates reverses the catalytic activity of nanoparticles , SM Rose, S Bedi, S Rakshit, S Sinha , Nanoscale , 2024 , 16(31) , 14730-14733 , https://doi.org/10.1039/D4NR01402B
  • 4.

    Doxorubicin catalyses self-assembly of p53 by phase separation , A Garg, G Kumar, V Singh, S Sinha , Current Research in Structural Biology , 2023 , 7 , 100133 , https://doi.org/10.1016/j.crstbi.2024.100133
  • 5.

    Innate and engineered attributes of bacterial microcompartments for applications in bio-materials science , SM Rose, A Radhakrishnan, S Sinha , Journal of Materials Chemistry. B , 2023 , - , 4842-4854 , https://doi.org/10.1039/D3TB00098B
  • 6.

    Self-assembly of Shell Protein and Native Enzyme in a Crowded Environment Leads to Catalytically Active Phase Condensates: , Gaurav Kumar, Sharmistha Sinha , (2023) , just accepted: just accepted , Biochemical Journal , 10.1042/BCJ20220551
  • 7.

    Disordered regions endow structural flexibility to shell proteins and function towards shell-enzyme interactions in propane diol utilization microcompartment: , Gaurav kumar, Jagadish Prasad Hazra, Sharmistha Sinha , (2022) , just accepted: , Journal of Biomolecular Structure & Dynamics
  • 8.

    Barrier-free liquid condensates of nanocatalysts as effective concentrators of catalysis: , Silky Bedi, Gaurav Kumar, S. M. Rose, Sabyasachi Rakshit, and Sharmistha Sinha , (2022) , 58: 8634-8637 , Chemical Communications , DOI https://doi.org/10.1039/D2CC03111F
  • 9.

    A Major Shell Protein of 1, 2‐Propanediol Utilization Microcompartment Conserves the Activity of Its Signature Enzyme at Higher Temperatures: , Gaurav Kumar, Naimat K. Bari,Jagadish P. Hazra,Dr. Sharmistha Sinha , (2022) , 23,: e2021006. , ChemBioChem , https://doi.org/10.1002/cbic.202100694
  • 10.

    Varying protein architectures in 3-dimensions for scaffolding and modulating properties of catalytic gold nanoparticles: , Simerpreet Kaur,Naimat K Bari,Sharmistha Sinha , (2022) , Just accepted: Just accepted , Amino Acids , 10.1007/s00726-022-03127-7
  • 11.

    Doxorubicin induced aggregation of α-synuclein: Insights into the mechanism of drug induced Parkinsonism: , Ankush Garg,Sharmistha Sinha , (2022) , 212: 112371. , Colloids and Surfaces B: Biointerfaces , 10.1016/j.colsurfb.2022.112371
  • 12.

    Biophysical approaches to understand and re-purpose bacterial microcompartments: , Gaurav Kumar,Sharmistha Sinha , (2021) , 63,: 43-51. , Current Opinion in Microbiology , 10.1016/j.mib.2021.05.008
  • 13.

    Factors deciding the assembly and thermostability of the DmrB cage: , Ankush Garg,Sharmistha Sinha , (2021) , 959-967, 182: 959-967 , International Journal of Biological Macromolecules 182
  • 14.

    Naturally occurring protein nano compartments: basic structure, function, and genetic engineering: , Dimple Goel,Sharmistha Sinha , (2021) , 2 (4): 042001 , Nano Express , 10.1088/2632-959X/ac2c93/
  • 15.

    Protein morphology drives the structure and catalytic activity of bio-inorganic hybrids: , Harpreet Kaur,Naimat K Bari,Ankush Garg,Sharmistha Sinha , (2021) , Just Accepted: , International Journal of Biological Macromolecules , 10.1016/j.ijbiomac.2021.01.217
  • 16.

    Temporal control in tritylation reactions through light-driven variation in chloride ion binding catalysis–A proof of concept: , Surbhi Grewal Saonli Roy Himanshu Kumar Mayank Saraswat Naimat K Bari Sharmistha Sinha Sugumar Venkataramani , (2020) , 10 (20): 7027-7033. , Catalysis Science & Technology , 10.1039/D0CY01090A
  • 17.

    Probe into a Multi-Protein Prokaryotic Organelle Using Thermal Scanning Assay Reveals Distinct Properties of the Core and the Shell: , Dr. Naimat K Bari ,Jagadish P Hazra ,Gaurav Kumar,Simerpreet Kaur,SHARMISTHA SINHA , (2020) , 1864(10): 129680 , BBA - General Subjects , 10.1016/j.bbagen.2020.129680
  • 18.

    Variable Mutations at the p53-R273 Oncogenic Hotspot Position Leads to Altered Properties: , Ankush Garg , Jagadish Prasad Hazra 2, Malay Kumar Sannigrahi 2, Sabyasachi Rakshit 3, Sharmistha Sinha , (2019) , 118 (3): 720-728 , Biophysical Journal , 10.1016/j.bpj.2019.12.015
  • 19.

    Functional protein shells fabricated from the self-assembling protein sheets of prokaryotic organelles: , Naimat K. Bari, Gaurav Kumar , Jagadish P. Hazra, Simerpreet Kaur ,Sharmistha Sinha , (2019) , 8: 523-533 , Journal of Materials Chemistry B , https://doi.org/10.1039/C9TB02224D
  • 20.

    Cellulose-metallothionein matrix for metal binding: , Naimat K.Bari ,Shaswat Barua ,Ankush Garg,Malay K Sannigrahi,Sharmistha Sinha , (2018) , 192: 126-134 , Carbohydrate polymers , 10.1016/j.carbpol.2018.03.043
  • 21.

    Nanoparticle Fabrication on Bacterial Microcompartment Surface for the Development of Hybrid Enzyme-Inorganic Catalyst.: , Naimat Kalim Bari , Gaurav Kumar, Aashish Bhatt, Jagadish Prasad Hazra, Ankush Garg, Md. Ehesan Ali , (2018) , 8: 7742–7748 , ACS Catal. , 10.1021/acscatal.8b02322
  • 22.

    The Wrappers of the 1,2-Propanediol Utilization Bacterial Microcompartments.: , Naimat K Bari, Gaurav Kumar, Sharmistha Sinha , (2018) , 1112: 333-344. , Adv Exp Med Biol , 10.1007/978-981-13-3065-0_23
  • 23.

    Enhanced bacterial cellulose production from Gluconobacter xylinus using super optimal broth: , Prathna T. Chandrasekaran, Naimat Kalim Bari , (2017) , 24(10): 4367–4381 , Cellulose
  • 24.

    Selective molecular transport through the protein shell of a bacterial microcompartment organelle: , Chowdhury C, Chun S, Pang A, Sawaya MR, Sinha S, Yeates TO, Bobik TA , (2015) , 112(10): 2990-5. , Proc Natl Acad Sci U S A. , 10.1073/pnas.1423672112
  • 25.

    Alanine scanning mutagenesis identifies an asparagine-arginine-lysine triad essential to assembly of the shell of the Pdu microcompartment: , Shouqiang Cheng, Yea Won Sung, Dan E. McNamara, Michael R. Sawaya, Todd O. Yeates, Thomas A. Bobik. J. , (2014) , 26(12): 2328-45. , J. Mol. Biol. , 10.1016/j.jmb.2014.04.012
  • 26.

    Diverse bacterial microcompartment organelles: , Chowdhury C, Sinha S, Chun S, Yeates TO, Bobik TA , (2014) , 78(3): 438-68 , Microbiol Mol Biol Rev , 10.1128/MMBR.00009-14
  • 27.

    A Key Role for Lysine Residues in Amyloid β-Protein Folding, Assembly, and Toxicity: , Sharmistha Sinha,Dahabada H. J. Lopes,Gal Bitan. ACS Chem. Neurosci. , (2012) , 3 (6): 473–481. , ACS Chem. Neurosci. , 10.1021/cn3000247
  • 28.

    Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments: , Sharmistha Sinha , (2012) , 109(37): 14995-5000. , PNAS , 10.1073/pnas.1207516109
  • 29.

    Comparison of Three Amyloid Assembly Inhibitors: The Sugar Scyllo-Inositol, the Polyphenol Epigallocatechin Gallate, and the Molecular Tweezer CLR01: , Sharmistha Sinha 1, Zhenming Du, Panchanan Maiti, Frank-Gerrit Klärner, Thomas Schrader, Chunyu Wang, Gal Bitan , (2012) , 3(6): 451-8. , ACS Chemical Neuroscience , DOI: 10.1021/cn200133x
  • 30.

    Lysine-Specific Molecular Tweezers Are Broad-Spectrum Inhibitors of Assembly and Toxicity of Amyloid Proteins: , Sharmistha Sinha, Dahabada H. J. Lopes, Zhenming Du, Eric S. Pang, Akila Shanmugam, Aleksey Lomakin, Peter Talbiersky, Annette Tennstaedt, Kirsten McDaniel, Reena Bakshi, Pei-Yi Kuo, Michael Ehrmann, George B. Benedek, Joseph A. Loo, Frank-Gerrit Klärner, Thomas Schrader, Chunyu Wang, and Gal Bitan J. Am. Chem. Soc , (2011) , 133 (42): 16958–16969. , J. Am. Chem. Soc. , 10.1021/ja206279b
  • 1.

    Application of Photochemical Cross-linking to the Study of Oligomerization of Amyloidogenic Proteins: , Lopes DHJ, C Rosensweig, G Bitan , (2012) , 849: 11-21 , Methods Mol Biol.
  • 2.

    Amyloids and Protein Aggregation—Analytical Methods: , Li H, F Rahimi, K Murakami, P Maiti, G Bitan , (2009) , Encyclopedia of Analytical Chemistry
  • 1.

    The 56th Biophysical Society Meeting: , SanDiego, CA , (2012)
  • 2.

    The 23rd Symposium of the Protein Society, Boston: , MA , (2009)
  • 3.

    XVII International Symposium on Glycoconjugates (GLYCO-17): , Bangalore , (2002)
  • 1. Xviii International Symposium On Glycoconjugates (glyco-18): , Florence, Italy, (2005)
  • 2. Molecular Tweezers For The Treatment Of Amyloid-related Diseases: , P. Talbiersky, A. Lomakin, F.-G. Klärner, T. Schrader, S. Frautschy,G. Bitan , (2010)
  • 3. New Compounds For The Treatment Of Diseases Related To Protein Misfolding: , T Schrader, K Hochdorffer, J Marz-Berberich, L Nagel-Steger, G Bitan , (2010)

  • Research Associate: Indian Institute of Science, Bangalore,, India (April 2007 to April 2008 )

  • Postdoctoral Fellow: Dept. of Neurology, University of California, Los Angeles,, USA (March 2008 to March 2010 )

  • Postdoctoral Fellow: Dept. of Biochem. Biophys. and Mol. Biol., Iowa State University, Ames,, USA (April 2010 to April 2013)

  • Title: Cell-free bioreactors from the shell proteins of bacterial microcompartments

    PI: Prof. Sharmistha Sinha

    Funding Amount: 47 lakhs

    Tenure: 3 years

    Funding Agency: SERB

  • Title: Cellulose-protein binary conjugates for metal detoxification

    PI: Prof. Sharmistha Sinha

    Funding Amount: 18 lakhs

    Tenure: 3 years

    Funding Agency: SERB-Women Excellence Award

  • Title: Exploring the shell proteins of BMCPs as potential substrate for fabrication of Organic-Inorganic Hybrid Nanomaterials

    PI: Prof. Sharmistha Sinha

    CO-PI: Prof. Ehesan Ali

    Funding Amount: 47 lakhs

    Tenure: 3 years

    Funding Agency: DST Nano Mission

  • Title: Understanding the Forces Involved in the Packing of Enzymes Inside the Bacterial Microcompartments for the Development of Novel Encapsulated Bio-Systems

    PI: Prof. Sharmistha Sinha

    Funding Amount: 58 lakhs

    Tenure: 3 years

    Funding Agency: DBT

  • Title: Biological treatment of engineered nanomaterials-contaminated wastewater-feasibility and implication

    PI: Dr. Sonalika Vaidya Role

    CO-PI: Prof. Sharmistha Sinha

    Funding Amount: 10 Lakhs (completed)

    Tenure: 2 years

    Funding Agency: INST