Krishnananda Chattopadhyay

Dr. Krishnananda Chattopadhyay

Principal Scientist
HOD, Structural Biology & Bioinformatics Division

Ph.D, Tata Institute of Fundamental Research, 2000
Research Associate (1999-2005), Washington University School of Medicine, St. Louis, USA ,
Senior Scientist (2005-2006), Pfizer Global Biologics, St. Louis, USA

    • Fluorescence Correlation Spectroscopy and Protein Folding
    • Protein Stability and Aggregation
    1. Sangeeta Kundu (Research Scientist) (
    2. Sunny Sharma (SRF) (
    3. Nidhi Joshi (Project Assistant) (
    4. Sujit Basak (SRF) (
    5. Suparna Sarkar (SRF) (
    6. Simanta Sarani Paul (SRF) (
    7. Pallabi Sil (SRF) (
    8. Amrita Kundu (JRF) (
    9. Sourav Chowdhury (JRF) (
    10. Sumanta Ghosh (JRF) (
    1. Ghosh S, Kundu A, Chattopadhyay K. Small Molecules Attenuate the Interplay between Conformational Fluctuations, Early Oligomerization and Amyloidosis of Alpha Synuclein. Sci Rep. 2018 Apr 3;8(1):5481. doi: 10.1038/s41598-018-23718-3.
    2. Sarkar-Banerjee S, Goyal S, Gao N, Mack J, Thompson B, Dunlap D, Chattopadhyay K, Finzi L. Specifically bound lambda repressor dimers promote adjacent non-specific binding. PLoS One. 2018 Apr 2;13(4):e0194930. doi: 10.1371/journal.pone.0194930. eCollection 2018.
    3. Chall S, Mati SS, Das I, Kundu A, De G, Chattopadhyay K. Understanding the Effect of Single Cysteine Mutations on Gold Nanoclusters as Studied by Spectroscopy and Density Functional Theory Modeling. Langmuir. 2017 Oct 31;33(43):12120-12129. doi: 10.1021/acs.langmuir.7b01789. Epub 2017 Oct 20.
    4. Singharoy D, Chowdhury S, Mati SS, Ghosh S, Chattopadhyay K, Bhattacharya SC. Photoinduced Electron Transfer Switching Mechanism of a Naphthalimide Derivative with its Solvatochromic Behaviour: An Experimental and Theoretical Study with In Cell Investigations. Chemistry. 2017 Nov 21;23(65):16516-16524. doi: 10.1002/chem.201702414. Epub 2017 Oct 26.
    5. Sannigrahi A, Maity P, Karmakar S, Chattopadhyay K. Interaction of KMP-11 with Phospholipid Membranes and Its Implications in Leishmaniasis: Effects of Single Tryptophan Mutations and Cholesterol. J Phys Chem B. 2017 Mar 2;121(8):1824-1834. doi: 10.1021/acs.jpcb.6b11948. Epub 2017 Feb 22.
    6. Kundu A, Kundu S, Chattopadhyay K. The presence of non-native helical structure in the unfolding of a beta-sheet protein MPT63. Protein Sci. 2017 Mar;26(3):536-549. doi: 10.1002/pro.3103. Epub 2017 Feb 12.
    7. Sil P, Paul SS, Silvio ED, Travaglini-Allocatelli C, Chattopadhyay K. Studies of cytochrome c-551 unfolding using fluorescence correlation spectroscopy and other biophysical techniques. Phys Chem Chem Phys. 2016 Sep 21;18(35):24537-48. doi: 10.1039/c6cp04819f. Epub 2016 Aug 19.
    8. Sarkar-Banerjee S, Chowdhury S, Paul SS, Dutta D, Ghosh A, Chattopadhyay K. The Non-native Helical Intermediate State May Accumulate at Low pH in the Folding and Aggregation Landscape of the Intestinal Fatty Acid Binding Protein. Biochemistry. 2016 Aug 16;55(32):4457-68. doi: 10.1021/acs.biochem.6b00390. Epub 2016 Aug 4.
    9. Paul SS, Sil P, Chakraborty R, Haldar S, Chattopadhyay K. Molecular Crowding Affects the Conformational Fluctuations, Peroxidase Activity, and Folding Landscape of Yeast Cytochrome c. Biochemistry. 2016 Apr 26;55(16):2332-43. doi: 10.1021/acs.biochem.6b00053. Epub 2016 Apr 14.
    10. Paul SS, Sil P, Haldar S, Mitra S, Chattopadhyay K. Subtle Change in the Charge Distribution of Surface Residues May Affect the Secondary Functions of Cytochrome c. J Biol Chem. 2015 Jun 5;290(23):14476-90. doi: 10.1074/jbc.M114.607010. Epub 2015 Apr 14.
    11. Mukherjee M, Ghosh R, Chattopadhyay K, Ghosh S. pH-induced structural change of a multi-tryptophan protein MPT63 with immunoglobulin-like fold: identification of perturbed tryptophan residue/residues. J Biomol Struct Dyn. 2015;33(10):2145-60. doi: 10.1080/07391102.2014.992043. Epub 2015 Jan 19.
    12. Joshi N, Basak S, Kundu S, De G, Mukhopadhyay A, Chattopadhyay K. Attenuation of the early events of α-synuclein aggregation: a fluorescence correlation spectroscopy and laser scanning microscopy study in the presence of surface-coated Fe3O4 nanoparticles. Langmuir. 2015 Feb 3;31(4):1469-78. doi: 10.1021/la503749e. Epub 2015 Jan 20.
    13. Basak S1, Prasad GV, Varkey J, Chattopadhyay K. Early sodium dodecyl sulfate induced collapse of α-synuclein correlates with its amyloid formation. ACS Chem Neurosci. 2015 Feb 18;6(2):239-46. doi: 10.1021/cn500168x. Epub 2014 Nov 17.
    14. Haldar S1, Sil P1, Thangamuniyandi M1, Chattopadhyay K1. Conversion of amyloid fibrils of cytochrome c to mature nanorods through a honeycomb morphology. Langmuir. 2015 Apr 14;31(14):4213-23. doi: 10.1021/la5029993. Epub 2014 Nov 5.
    15. Basak S1, Chattopadhyay K. Studies of protein folding and dynamics using single molecule fluorescence spectroscopy. Phys Chem Chem Phys. 2014 Jun 21;16(23):11139-49. doi: 10.1039/c3cp55219e. Epub 2014 May 8.
    16. Sarkar S1, Chattopadhyay K. Studies of early events of folding of a predominately β-sheet protein using fluorescence correlation spectroscopy and other biophysical methods. Biochemistry. 2014 Mar 11;53(9):1393-402. doi: 10.1021/bi4014837. Epub 2014 Feb 27.
    17. Lahiri S, Banerjee S, Dutta T, Sengupta S, Dey S, Roy R, Sengupta D, Chattopadhyay K, Ghosh AK. Enzymatic and regulatory attributes of trehalose-6-phosphate phosphatase from Candida utilis and its role during thermal stress. J Cell Physiol. 2014 Sep;229(9):1245-55. doi: 10.1002/jcp.24562. PMID: 24446217
    18. Sharma, S., Sarkar, S., Paul, S.S., Roy, S. & Chattopadhyay, K. A small molecule chemical chaperone optimizes its unfolded state contraction and denaturant like properties. Sci. Rep. 3, 3525; DOI:10.1038/srep03525 (2013).
    19. Basak S, Chattopadhyay K. Fluorescence Correlation Spectroscopy Study on the Effects of the Shape and Size of a Protein on Its Diffusion Inside a Crowded Environment. Langmuir. 2013 Nov 14. [Epub ahead of print]
    20. Nidhi Joshi , Anindita Mukhopadhyay , Sujit Basak , Goutam De , and Krishnananda Chattopadhyay. Surface Coating Rescues Proteins from Magnetite Nanoparticle Induced Damage. Part. Part. Syst. Charact. 2013, 30, 683–694
    21. Sunny Sharma, Nikhil Pathak, Krishnananda Chattopadhyay. Osmolyte induced stabilization of protein molecules: A Brief Review, Journal of Proteins and Proteomics. 2012; 3(2):129-139.
    22. Ghosh R, Mukherjee M, Chattopadhyay K, Ghosh S. Unusual optical resolution of all four tryptophan residues in MPT63 protein by phosphorescence spectroscopy: assignment and significance. J Phys Chem B. 2012 Oct 18;116(41):12489-500.
    23. Haldar, S., & Chattopadhyay, K. (2012) The interconnection of salt induced hydrophobic compaction and secondary structure formation depends on solution conditions: revisiting early events of protein folding at single molecule resolution. Journal of Biological Chemistry VOL. 287, NO. 14, pp. 11546–11555, March 30, 2012
    24. Haldar, S., Paul, S. S., Joshi, N., Dasgupta, A., Chattopadhyay, K., (2012) The Presence of the Iron-Sulfur Motif Is Important for the Conformational Stability of the Antiviral Protein, Viperin. Plos One Volume 7 | Issue 2 | e31797.
    25. Lahiri, S., Basu, A., Sengupta, S., Banerjee, S., Dutta, T., Soren, D., Chattopadhyay, K., Ghosh, A. K., Purification and characterization of a trehalase–invertase enzyme with dual activity from Candida utilis (2012) Archives of Biochemistry and Biophysics Volume 522, Issue 2, Pages 90–99.
    26. Mukhopadhyay A, Joshi N, Chattopadhyay K, De G. (2011) A facile synthesis of PEG-coated magnetite (Fe3O4) nanoparticles and their prevention of the reduction of cytochrome c. ACS Appl Mater Interfaces. 2012 Jan;4(1):142-9. Epub 2011 Dec 9.
    27. Sen, T., Mandal, S., Haldar, S., Chattopadhyay, K., and Patra, A., (2011) J. Phys. Chem. C, 115 (49), pp 24037–24044.
    28. Haldar, S., & Chattopadhyay, K. (2011) Effects of arginine and other solution additives on the self-association of different surfactants: an investigation at single molecule resolution. Langmuir 27, 5842-5849
    29. Mukhopadhyay, A, Basak, S., Das, JK, Chattopadhyay, K. & De, G (2010) Ag-TiO2 nanoparticle co-doped SiO2 films on ZrO2 barrier-coated glass substrates with antibacterial activity in ambient condition. ACS Appl Mater Interfaces 9, 2540-6.
    30. Haldar, S, Mitra, S. & Chattopadhyay, K (2010) The role of the protein stabilizers on the conformations of the unfolded states and its early folding kinetics: An investigation at single molecular resolution. Journal of Biological Chemistry 285, 25314-23.
    31. Ghosh, R., Sharma, S. & Chattopadhyay, K.(2009) Effect of Arginine on Protein Aggregation Studied by Fluorescence Correlation Spectroscopy and Other Biophysical Methods, Biochemistry 48 (5), 1135 – 1143.
    32. Chattopadhyay, K. & Frieden, C. (2006) Steady State and Time-resolved fluorescence studies of the intestinal fatty acid binding proteins, Proteins 63, 327-335.
    33. Chattopadhyay, K., Elson, E. L., & Frieden, C. (2005) Measurements of microsecond dynamics of the unfolded state by using fluorescence methods, Proc. Natl. Acad. Sci (USA) 102, 2385-2389.
    34. Chattopadhyay, K., Saffarian, S., Elson, E. L., & Frieden, C, (2005) Measuring unfolding of proteins in the presence of denaturant using fluorescence correlation spectroscopy. Biophysical Journal 88, 1413-1422.
    35. Chattopadhyay, K., & Mazumdar, S. (2003) Stabilization of partially folded states of cytochrome c in aqueous micelles: effects of ionic and hydrophobic interactions. Biochemistry 42, 14606-14613.
    36. Chattopadhyay, K.; Saffarian, S.; Elson, E. L.; & Frieden, C. (2002) Measurement of microsecond dynamic motion in the intestinal fatty acid binding protein by using fluorescence correlation spectroscopy. Proc. Natl. Acad. Sci. (USA), 99, 14171 – 14176.
    37. Frieden, C.; Chattopadhyay, K.; & Elson, E.L; (2002) What Fluorescence Correlation Spectroscopy can tell us about unfolded state of a protein. Adv. Prot. Chem., 62, 91-109.
    38. Chattopadhyay, K; Das, T. K; Majumdar, A; & Mazumdar, S (2002) NMR studies on interaction of lauryl maltoside with cytochrome c oxidase: a model for surfactant interaction with the membrane protein. J. Inor. Biochem 91, 116-124.
    39. Chattopadhyay, K.; Zhong, S.; Yeh, S. R.; Rousseau, D., L; & Frieden, C. (2002) The Intestinal Fatty Acid Binding Protein: the role of turns in fast and slow folding processes. Biochemistry 41, 4040-4047.
    40. Chattopadhyay, K.; & Mazumdar, S. (2001) Direct electrochemistry of heme proteins: effect of electrode surface modification by neutral surfactants. Bioelectrochemistry 53, 17-24.
    41. Chattopadhyay, K.; & Mazumdar, S. (2000) Structural and conformational stability of horseradish peroxidase: effect of temperature and pH. Biochemistry 39, 263-270.
    42. Chattopadhyay, K.; &Mazumdar, S. (1999) Direct electrochemical oxidation of horseradish peroxidase: cyclic voltammetric and spectroelectrochemical studies. New J Chem 23, 137-139.