** indicates Corresponding Author papers
** "Deep Eutectic Solvent-Assisted Carbon Quantum Dots for Nanomolar Detection of 4-Nitrophenol", M. Kaur, M. Bhattacharya* and B. Maity* RSC Adv. 2025, (In press)
** "Regulating aggregation of an intrinsically disordered chaperone-like casein", J. Kaur and M. Bhattacharya* J. Colloid Interface Sci. 2025, 697, 137916.
** "Preferential Binding of Cations Modulates Electrostatically-Driven Protein Aggregation and Disaggregation", D. Singla and M. Bhattacharya* J. Phys. Chem. B 2024, 128, 10870-10879.
** "Intrinsic conformational preference in the monomeric protein governs amyloid polymorphism", A. Giri and M. Bhattacharya* Phys. Chem. Chem. Phys. 2024, 26, 25222-25231.
https://pubs.rsc.org/en/Content/ArticleLanding/2024/CP/D4CP01973C
** "Green transformation of biomass-derived Indian gooseberry into fluorescent intrinsic nitrogen-functionalized carbon quantum dots for real-time detection of vitamin B2 in the nanomolar range", M. Kaur, M. Bhattacharya*, and B. Maity* RSC Sustain. 2024, 2, 1472-1486.
https://pubs.rsc.org/en/Content/ArticleLanding/2024/SU/D3SU00456B
** "Deciphering conformational changes in human serum albumin induced by bile salts using spectroscopic and molecular modeling approaches", M. Kaur, M. Bhattacharya*, and B. Maity* J. Mol. Liq. 2023, 390, 123026.
https://www.sciencedirect.com/science/article/pii/S0167732223018329
** “Salt-induced dissolution of protein aggregates”, D. Singla and M. Bhattacharya* J. Phys. Chem. B 2022, 126, 8760-8770.
https://pubs.acs.org/doi/abs/10.1021/acs.jpcb.2c06555
** “The protein–surfactant stoichiometry governs the conformational switching and amyloid nucleation kinetics of tau K18”, J. Kaur, A. Giri, and M. Bhattacharya* Eur. Biophys. J. 2020, 49, 425-434.
https://link.springer.com/article/10.1007/s00249-020-01447-8
** “pH-responsive mechanistic switch regulates the formation of dendritic and fibrillar nanostructures of a functional amyloid”, P. Dogra, M. Bhattacharya* and S. Mukhopadhyay* J. Phys. Chem. B 2017, 121, 412-419.
http://pubs.acs.org/doi/abs/10.1021/acs.jpcb.6b11281
"Water rearrangements upon disorder-to-order amyloid transition", S. Arya, A.K. Singh, T. Khan, M. Bhattacharya, A. Datta, and S. Mukhopadhyay J. Phys. Chem. Lett. 2016, 7, 4105-4110.
http://pubs.acs.org/doi/abs/10.1021/acs.jpclett.6b02088
"Direct observation of the intrinsic backbone torsional mobility of disordered proteins", N. Jain, D. Narang, K. Bhasne, V. Dalal, S. Arya, M. Bhattacharya, and S. Mukhopadhyay Biophys. J. 2016, 111, 768-774.
http://www.cell.com/biophysj/fulltext/S0006-3495(16)30589-6
"Conformational switching and nanoscale assembly of human prion protein into polymorphic amyloids via structurally-labile oligomers", V. Dalal, S. Arya, M. Bhattacharya, and S. Mukhopadhyay Biochemistry 2015, 54, 7505-7513.
http://pubs.acs.org/doi/abs/10.1021/acs.biochem.5b01110
** “Self-assembly of ovalbumin amyloid pores: Effects on membrane permeabilization, dipole potential and bilayer fluidity”, M. Bhattacharya*, and P. Dogra Langmuir 2015, 31, 8911-8922.
http://pubs.acs.org/doi/abs/10.1021/acs.langmuir.5b02074
** “Appearance of annular ring-like intermediates during amyloid fibril formation from human serum albumin”, S. Arya, A. Kumari, V. Dalal, M. Bhattacharya*, and S. Mukhopadhyay* Phys. Chem. Chem. Phys. 2015, 17, 22862-22871.
http://pubs.rsc.org/en/content/articlelanding/2015/cp/c5cp03782d
** “Nanophotonics of protein amyloids”, M. Bhattacharya*, and S. Mukhopadhyay* Nanophotonics 2014, 3, 51-59.
http://www.degruyter.com/view/j/nanoph.2014.3.issue-1-2/nanoph-2013-0045/nanoph-2013-0045.xml
** “Nanoscopic amyloid pores formed via stepwise protein assembly”, M. Bhattacharya*, N. Jain, P. Dogra, S. Samai and S. Mukhopadhyay* J. Phys. Chem. Lett. 2013, 4, 480-485.
http://pubs.acs.org/doi/abs/10.1021/jz3019786
** “Structural and dynamical insights into the molten-globule form of Ovalbumin”, M. Bhattacharya* and S. Mukhopadhyay* J. Phys. Chem. B 2012, 116, 520-531.
http://pubs.acs.org/doi/abs/10.1021/jp208416d
“Nanoscale fluorescence imaging of single amyloid fibrils”, V. Dalal*, M. Bhattacharya*, D. Narang, P.K. Sharma, and S. Mukhopadhyay J. Phys. Chem. Lett. 2012, 3, 1783-1787. *Joint first author
http://pubs.acs.org/doi/abs/10.1021/jz300687f
“Chain collapse of an amyloidogenic intrinsically disordered protein”, N. Jain*, M. Bhattacharya* and S. Mukhopadhyay Biophys. J. 2011, 101, 1720-1729. *Joint first author.
http://www.cell.com/biophysj/retrieve/pii/S0006349511009702
Featured as a ‘Must Read’ article in the Faculty of 1000 (http://f1000.com/13409028)
“Insights into the mechanism of aggregation and fibril formation from Bovine Serum Albumin”, M. Bhattacharya, N. Jain and S. Mukhopadhyay J. Phys. Chem. B 2011, 115, 4195–4205.
http://pubs.acs.org/doi/abs/10.1021/jp111528c
“pH-induced conformational isomerization of bovine serum albumin studied by extrinsic and intrinsic protein fluorescence”, M. Bhattacharya, N. Jain, K. Bhasne, V. Kumari and S. Mukhopadhyay J. Fluorescence 2011, 21, 1083-1090.
http://www.springerlink.com/content/g56h4hk23663q734/
“Kinetics of surfactant-induced aggregation of lysozyme studied by fluorescence spectroscopy” N. Jain, M. Bhattacharya and S. Mukhopadhyay J. Fluorescence 2011, 21, 615-625.
http://www.springerlink.com/content/f8662237w17652h2/
“Quadratic nonlinearity of one- and two-electron oxidized metalloporphyrins and its switching in solution”, A. Wahab, M. Bhattacharya, S.Ghosh, A.G. Samuelson and P. K. Das. J. Phys. Chem. B. 2008, 112, 2842-2847.
http://pubs.acs.org/cgi-bin/abstract.cgi/jpcbfk/2008/112/i10/abs/jp076909m.html
“Enhancement of quadratic nonlinearity via multiple hydrogen bonded supramolecular complex formation”, M. Bhattacharya, A.G. Samuelson and P. K. Das J. Phys. Chem. B 2007, 111, 7122-7126.
http://pubs.acs.org/cgi-bin/abstract.cgi/jpcbfk/2007/111/i25/abs/jp0721651.html
“Second order nonlinearity in oligoamides”, M. Bhattacharya and P. K. Das Synth. Met. 2005, 155, 389-392.
http://dx.doi.org/10.1016/j.synthmet.2005.09.020
“Synthesis and nonlinear optical properties of some donor-acceptor oxadiazoles”, S. H. Mashraqui, R. S. Kenny, S. G. Ghadigaonkar, A. Krishnan, M. Bhattacharya and P. K. Das, Opt. Mater. 2004, 27, 257-260.
http://dx.doi.org/10.1016/j.optmat.2004.04.006
Book Chapters
"Studying protein misfolding and aggregation using fluorescence spectroscopy" M. Bhattacharya, and S. Mukhopadhyay Reviews in Fluorescence 2015, C. D. Geddes (Ed.), Springer, Switzerland, pp. 1-27.
“Nonlinear Optical Properties of Organometallic and Metalloorganic Compounds”, M. Bhattacharya, P. K. Das and A. G. Samuelson, in Handbook of Organic Electronics and Photonics, 2008 H. S. Nalwa (Ed.) Vol. 2, American Scientific Publishers, California, USA.