Neha Jain

Assistant Professor
Areas of interest
Amyloids, Biofilms, Neurodegeneration, Molecular Biophysics, Microbiology

Dr Neha Jain is an Assistant Professor in the Biological and Life Sciences division of the School of Arts and Sciences. She did an MSc in Industrial Microbiology at the University of Rajasthan, Jaipur, and a PhD in Molecular Biophysics at the Indian Institute of Science Education and Research, Mohali (IISER Mohali). Her PhD work was focused on understanding the mechanism of amyloid formation in different proteins involved in neurodegenerative diseases such as Parkinson’s and Alzheimer’s diseases (Jain et al; Biophys J 2011 and Biophys J 2016).

Following her PhD, Dr Jain joined the University of Michigan, Ann Arbor, as a postdoctoral research fellow. Her work was focused on understanding the molecular basis of curli (bacterial functional amyloid) inhibition. She implemented small molecules and chaperone-like proteins to reduce biofilm burden. In an effort to develop new strategies to combat antibiotic resistance, she discovered that a human protein, transthyretin, can inhibit bacterial amyloid (curli) formation in vitro and biofilm-formation in vivo (Jain et al, Proc Natl Acad Sci USA 2017).

At Ahmedabad University, Dr Jain intends to develop her studies to understand the effects of bacterial amyloids on human diseases. Her laboratory uses a wide range of microbiological, biophysical and biochemical techniques to answer the questions.

Research at the Jain lab is primarily curosity and question driven. At present, we are focusing on following areas, however we welcome new ideas and collaborations to expand our research area:

1. Development of strategies to combat amyloid-dependent biofilm formation

2. Role of microbial amyloids in non-microbial diseases

3. Cross-talk between amyloids of different origin and its consequences

Articles in peer reviewed journals:

1. Jain N, Ådén J, Nagamatsu K, Evans ML, Li X, McMichael B, Ivanova MI, Almqvist F, Buxbaum JN, and Chapman MR (2017). Inhibition of Curli Assembly and E. coli Biofilm Formation by the Human Systemic Amyloid Precursor Transthyretin. Proc Natl Acad Sci U S A. 2017 Oct 30. pii: 201708805. doi: 10.1073/pnas.1708805114. [Epub ahead of print].

2. Arya S, Dogra P, Jain N and Mukhopadhyay S. Detergent-induced Aggregation of an Amyloidogenic Intrinsically Disordered Protein. Accepted at Journal of Chemical Sciences.

3. Jain N, Narang D, Bhasne K, Dalal V, Arya S, Bhattacharya M, and Mukhopadhyay S (2016). Direct observation of the intrinsic backbone torsional mobility of disordered proteins. Biophys. J.111:768–774.

4. Horowitz S, Koepnick B, Martin R, Tymieniecki A, Winburn A, Cooper S, Flatten J, Rogawski D, Koropatkin N, Hailu T, Jain N, Chapman MR, Sikkema A, Skiba M, Maloney F, Beinlich F, Players F, Students UM, Popovi? Z , Baker D, Khatib F, and Bardwell JCA (2016). Determining crystal structures through crowdsourcing and coursework. Nat. Commun. 7:12549.

5. Taylor JD, Hawthorne WJ, Lo J, Dear A, Jain N, Meisl G, Andreasen M, Fletcher C, Koch M, Darvill N, Scull N, Escalera-Maurer A, Sefer L, Wenman R, Lambert S, Jean J, Xu Y, Turner B, Kazarian SG, Chapman MR, Bubeck D, de Simone A, Knowles TP, Matthews SJ (2016). Electrostatically-guided inhibition of curli amyloid nucleation by the CsgC-like family of chaperones. Sci. Rep. 6:24656.

6. Chorell E, Andersson E, Evans ML, Jain N, Götheson A, Åden J, Chapman MR, Almqvist F, and Wittung-Stafshede P (2015). Bacterial chaperones CsgE and CsgC differentially modulate human α-synuclein amyloid formation via transient contacts. PLoS ONE 10(10): e0140194.

7. Jain N, Bhasne K, Hemaswasthi M, and Mukhopadhyay S (2013). Structural and dynamical insights into the membrane-bound α-Synuclein. PLoS ONE 8(12):e83752.

8. Bhattacharya M*, Jain N*, P. Dogra, S. Samai and S. Mukhopadhyay (2013). Nanoscopic amyloid pores formed via stepwise protein assembly. J. Phys. Chem. Lett. 4:480-485. *Joint first author.

9. Jain N, Bhattacharya M, and Mukhopadhyay S (2011). Chain collapse of an amyloidogenic intrinsically disordered protein. Biophys. J. 101:1720-1729.

10. Bhattacharya M, Jain N, and Mukhopadhyay S (2011). Insights into the mechanism of aggregation and fibril formation from bovine serum albumin. J. Phys. Chem. B 115:4195–4205.

11. Bhattacharya M, Jain N, Bhasne K, Kumari V and Mukhopadhyay S (2011). pH-induced conformational isomerization of bovine serum albumin studied by extrinsic and intrinsic protein fluorescence. J. Fluoresc. 21:1083-1090.

12. Jain N, Bhattacharya M and Mukhopadhyay S (2011). Kinetics of surfactant-induced aggregation of lysozyme studied by fluorescence spectroscopy. J. Fluoresc. 21:615-625.

13. Kumar S, Jain N and Mukherjee TK (2009). Role of RAGE in idiopathic pulmonary ?brosis:Promising prospects. Resp. Physiol. Neurobiol. 165:121–122.

14. Shivaprakash MR, Jain N, Gupta S, Baghela A, Gupta A and Chakrabarti A (2009). Allergic fungal rhinosinusitis caused by Neosartorya hiratsukae from India. Medical Mycology 1-4.

Book chapters:

  1. Jain N, Hammer ND, Wang X, McGuffie BA, and Chapman MR (2017). Amyloid: Friend and Foe. Handbook of Infection and Alzheimer’s disease J. Miklossy (Ed.) IOS Press (5) 297-311.
  2. Jain N and Mukhopadhay S (2015). Applications of fluorescence anisotropy in understanding protein conformational disorder and aggregation. Applied Spectroscopy and the Science of Nanomaterials. Progress in Optical Science and Photonics. 8:41-57.


Currently, I am offering following courses:

1. GE221 Ethics in Life Sciences (Bioethics)

If your research interests broadly matches with ours, please write to me. Currently, I am accepting applications from:

Ph.D. candidates : admission through Ahmedabad University.

Postdoctoral Fellows: I do not have funds to support postdoctoral fellows as of now. However, if you are really interested, I can help in finding an extramural funding to support your proposal.


Centre of Excellence, Division of Biological & Life Sciences,
Ahmedabad University,
Central Campus,
Navrangpura, Ahmedabad,
Gujarat, India


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