Anirban Bhunia
Associate Professor

 Contact

 Office: Annex building, 2nd floor
Telephone: +91-33-25693336
E-mail: bhunia@jcbose.ac.in or anirbanbhunia@gmail.com 

Education 

M.Sc (Biotechnology), Indian Institute of Technology, Bombay.
Ph.D (Chemistry), University of Luebeck Germany. 

Group Page

Research interest 

The main focus of my lab is to use the application of state-of-the art NMR spectroscopy and other biophysical methods, including CD, Fluorescence etc. in conjunction with molecular modeling techniques to address the following projects:

  1. Designing of novel antifreeze peptides with potential applications in many areas such as medicine, agriculture and industry.
  2. Receptor-ligand interaction study to develop structure based drug design.
  3. Novel Antimicrobial peptides (AMPs) to develop antimicrobial and antisepsis drugs.
  4. Structure and dynamics study of amyloid beta (Ab40) protein in micelle environment.
  5. Designing of novel cell penetrating peptides (CPPs) and its function for drug delivery.
  6. Structure-function correlation for Myelin-Associated Glycoprotein (MAG), responsible for inhibition of axon regeneration in the central nervous system (CNS).
  7. DNA-antimicobial peptide (AMP) interaction study to understand the mechanism of action for AMPs to kill the bacteria.
  8. de novo designed small loop to stop protein aggregation.
  9. Structure determination of c-terminal of Raf1 kinase: Implications in a signaling pathway.
  10. Exploring the self-assembly of short peptides: Applications to nanoparticle/hydrogels/fibrillation.


Open Position


LIST OF PUBLICATIONS (*corresponding author) 

2016

55. Mangoni ML, Bhunia A*, (2016) Editorial: Antimicrobial Peptides in Medicinal Chemistry: Advances and Applications. Curr Top Med Chem, 16, 2-3.

54. Sharma S, Sahoo N, Bhunia A*, (2016) Antimicrobial Peptides and their Pore/Ion Channel Properties in Neutralization of Pathogenic Microbes. Curr Top Med Chem, 16, 42-53.

2015

53. Pithadia AS, Bhunia A, Sribalan R, Padroni V, Fierce CA, Ramamoorthy A (2015) Influence of a Curcumin Derivative on hIAPP aggregation in the Absence and Presence of Lipid MembraneChemComm. Just accepted

52. Korshavn K, Jang M, Kwak YJ, Kochi A, Vertuani S, Bhunia A, Manfredini S, Ramamoorthy A, Lim MH (2015) Reactivity of Metal-Free and Metal-Associated Amyloid-beta with Glycosylated Polyphenols and Their Esterified Derivatives. Nature Sci. Rep. Just accepted

51. Korshavn K, Bhunia A, Lim MH, Ramamoorthy A, (2015) Ab40 Adopts a Conserved, Partially Folded Structure upon Binding to Zwitterionic Bilayers Prior to Amyloid Formation. ChemComm. Just accepted

50. Datta A, Kundu P, Bhunia A* (2015) Designing potent antimicrobial peptides by disulphide linked dimerization and N-terminal lipidation to increase antimicrobial activity and membrane perturbation: Structural insights into lipopolysaccharide binding. J. Colloid Interface Sci., 461, 335-345.
49. 
Kar RK, Bhunia A* (2015) Biophysical and Biochemical Aspects of Antifreeze Proteins: Using Computational Tools to Extract Atomistic Information. Progress Biophys. Mol. Biol., 119, 194-201.

48. Kar RK, Bhunia A* (2015) Will It Be Beneficial to Simulate The Antifreeze Proteins at Ice Freezing Condition or at Lower Temperature? J. Phys. Chem B119, 11485-95.
47
. Ghosh A, Ratha BN, Gayen N, Mroue KH, Kar RK, Mandal AK*, Bhunia A* (2015) Biophysical Characterization of Essential Phosphorylation at the Flexible C-terminal Region of C-Raf with 14-3-3ζ Protein. PLOS One, 10 (8), e0135976.

46. Datta A, Ghosh A, Airoldi C, Sperandeo P, Mroue KH, Barbero JJ, Kundu P, Ramamoorthy A, Bhunia A* (2015)Antimicrobial peptides: Insight into Membrane Permeabilization, Lipopolysaccharide Fragments and Application in Plant Disease Control. Nature Sci. Rep.5, 11951.

45. Gupta S, Chit JC-Y, Feng C, Bhunia A, Tan S-M, Bhattacharjya S (2015) An Alternative phosphorylation switch in Integrin b2 (CD18) tail for DOK1 binding. Nature Sci. Rep., 5, 11630. 

44. Bera S, Ghosh A, Sharma S, Debnath T, Giri B, Bhunia A* (2015) Probing the role of Proline in the Antimicrobial activity and lipopolysaccharide binding of Indolicidin. J Colloid Interface Sci.452, 148-159.

43. Ghosh A, Pithadi A, Bhat J, Bera S, Midya A, Fierke C, Ramamoorthy A, Bhunia A*, (2015) Self-assembly of a 9-residue amyloid-forming peptide fragment of SARS Corona Virus E-protein: Mechanism of self aggregation and amyloid inhibition of hIAPP. Biochemistry, 54, 2249 -2261

42. Lee DK, Bhunia A, Kotler SA, Ramamoorthy A* (2015) Antimicrobial peptides and inhibition by cholesterol: A solid-state Nuclear Magnetic Resonance study. Biochemistry, 54, 1897-907.

41.  Nandi SK, Chakraborty A, Panda AK, Ray SS, Kar RK, Bhunia A, Biswas A* (2015) Interaction of ATP with a small heat shock protein from Mycobacterium leprae: Effect on its structure and function.  PLOS Negl. Trop. Diseas., 9, e0003661.

40. Sudheendra US, Dhople V, Datta A, Kar RK, Shelburne CE, Bhunia A*, Ramamoorthy A*  (2014) Membrane Disruptive Antimicrobial Activities of Human beta defensin-3 Analogs. Eur. J. Med. Chem., 91, 91-99.

2014

39. DiMauro MA, Nandi SK, Raghavan CT, Kar RK, Wang B, Bhunia A, Nagaraj RH*, Biswas A* (2014) Acetylation of Gly1 and Lys2 promotes aggregation of human ?D-crystallin. . Biochemistry, 53(46), 7269-82.

38. Ghosh T, Kar RK, Bhunia A, Misra A* (2014) Synthesis of the pentasaccharide repeating unit of the O-antigen of E.coli 0175 using one-pot glycosylation and its conformational analysis. . Tetrahedron, 53(46), 7269-82.

37. Jana M, Kar RK, Bhunia A, Misra A* (2014) Synthesis of the tetrasaccharide repeating unit of the O-antigen of the Escherichia coli O69 strain and its conformational analysis.. RSC Adv., 4, 079-84.

36. Ghosh A, Kar RK, Krishnamoorthy J, Chatterjee S*, Bhunia A* (2014) Double GC:GC Mismatch in dsDNA Enhances Local Dynamics Retaining the DNA Footprint: A High-Resolution NMR Study. ChemMedChem., 9(9), 2052-58.(invited paper) .

35. Ghosh A, Kar RK, Jana J, Saha A, Jana B, Krishnamoorthy J, Kumar D, Ghosh S*, Chatterjee S*, Bhunia A* (2014) Indolicidin Targets Duplex DNA: Structural and Mechanistic Insights Employing Combination of Spectroscopy and Microscopy. ChemMedChem. 9(9), 2059-64(invited paper).

34. Dhara D, Kar RK, Bhunia A*, Misra AK*  (2014) Convergent Synthesis and Conformational Analysis of the Hexasaccharide Repeating Unit of the O-Antigen of Shigella flexneri Serotype 1D. Eur. J. Org. Chem. 2014, 4577-84.,

33. Ravichandran Y, Krishnamoorthy J, Ramamoorthy A*, Bhunia A* (2014) Potent gamma-secretase inhibitors/modulators interacts with Amyloid-beta fibrils but do not inhibit fibrillation: A high resolution NMR study Biochem. Biophys. Res. Comm.447(4), 590 -5.

32. Ghosh A, Datta A, Jana J, Kar RK, Chatterjee C, Chatterjee S*, Bhunia A*(2014) Sequence context induced antimicrobial activity: Insight to Lipopolysaccharide permeabilization. Mol. Biosyst.10(6), 1596-612.

31. Santra A, Si A, Kar RK, Bhunia A*, Mishra AK*  (2014) Linear synthesis and conformational analysis of the pentasaccharide repeating unit of the cell wall O-antigen of Escherichia coli O13. Carbohydr. Res.391, 9-15.

2013

30. Saravanan R, Joshi M, Mohanram H, Bhunia A, Bhattacharjya S (2013)* NMR structure of temporin-1 ta in lipopolysaccharide micelles: mechanistic insight into inactivation by outer membrane. .PLOS One, 8(9), e72718.

29.  Banejee V3, Kar RK1, Datta A, Parthasarathi K, Chatterjee S, Das KP*, Bhunia A*,  (2013) Use of Small Peptide Fragment as an Inhibitor of Insulin Fibrillation Process: A Study by High and Low Resolution Spectroscopy. PLOS One, 8(8), e72318. ( 1 both authors contributed equally)

28.      Jana J, Kar RK, Ghosh A, Biswas A, Ghosh S, Bhunia A*, Chatterjee S* (2013) Human Cathelicidin Peptide LL37 Bind Telomeric G-Quadruplex. Mol. Biosys. 9(7), 1833-6 9(7):1833-6.

27.      Kar RK, Suryadevara P, Jana J, Bhunia A*, Chatterjee S* (2013) Novel G-quadruple Stabilizing Agents: In-silico Approach and Dynamics. J. Biomol. Str. Dynam. (In press).

2012

26.      Shah SHH1, Kar RK1, Asmawi AA, Rahman MBA, Murad AMA, Mahadi NM, Basri M, Rahman RNZAR, Salleh AB, Chatterjee S*, Tejo BA*, Bhunia A* (2012) Solution Structures, Dynamics, and Ice Growth Inhibitory Activityof Peptide Fragments Derived from an Antarctic Yeast Protein. PLOS One, 7(11), e49788.                  ( 1 both authors contributed equally)

25. Mohanram H, Nip A, Domadia PN, Bhunia A, Bhattacharjya S. (2012) NMR structure, localization, and vesicle fusion of chikungunya virus fusion Peptide. Biochemistry, 51(40), 7863-72.

24. Bhunia A, Mohanram H, and Bhattacharjya S. (2012) Structural Determinants of the Specificity of a Membrane Binding Domain of the Scaffold Protein Ste5 of Budding Yeast: Implications in Signaling by the Scaffold Protein in MAPK Pathway. Biochim. Biophys. Acta, 1818(5), 1250-60.

23. Bhunia A*, Bhattacharjya S, Chatterjee, S. (2012) Applications of Saturation Transfer Difference (STD) NMR in Biological Systems. Drug Discov. Today, 17(9-10), 505-13.

2011

22. Bhunia A, Saravanan R, Mohanram H, Mangoni ML, Bhattacharjya S. (2011) NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide Micelles: mechanistic insights into outer membrane permeabilization and synergistic activity. J Biol Chem., 286(7), 24394-406.

2010

21. Domadia PN, Bhunia A, Ramamoorthy A, Bhattacharjya S. (2010) Structure, Interactions, and Antibacterial activities of MSI-594 derived mutant peptie MSI-594F5A in Lipolysaccharide Micelles: Role of the Helical Hairpin Conformation in Outer-Membrane Permeabilization. J. Am. Chem. Soc., 132 (51), 18417-28.

20. Bhunia A, Vivekanandan S, Eckert T, Burg-Roderfeld M, Wechselberger R, Romanuka J, Bäle D, Kornilov AV, von der Leith C-W, Barbero JJ, Nifantiev N, Schachner M, Sewald N, Lü T, Gabius, H-J, Siebert H-C. (2010) Why the structurally different cyclic peptides can be glycomemtics of HNK-1? J. Am. Chem. Soc, 132, 96-105.

19. Bhunia A, Bhattacharjya S. (2010) Mapping Residue Specific Contacts of Polymyxin B with Lipopolysaccharide by Saturation Transfer Difference (STD) NMR: Insights into Outer-membrane Disruption and Endotoxin Neutralization. Biopolymers, 96, 273-287.

18. Bhunia A, Domadia PN, Torres J, Ramamoorthy A, Bhattacharjya S. (2010) NMR Structure of Pardaxin, a Pore-Forming Antimicrobial Peptide, in Lipopolysaccharide Micelles: Mechanism of Outer membrane Permeabilization. J. Biol. Chem., 285(6), 3883-95.

17. Domadia PN, Li YF, Bhunia A, Mohanram H, Tan SM, Bhattacharjya S. (2010) Functional and structural characterization of the talin F0F1 domain. Biochem. Biophys. Res. Commun. 391(1), 159-65.

16. Rathi S, Bhunia A, Bhattacharjya S. (2010) Role of the Central Hinge Region in the Structure and Activity of Melittin: Designing Non-toxic Antisepsis/Antimicrobial Agents. Biochim. Biophys. Acta, 1798(2), 128-139. (Invited Paper)

2009

15. Bhunia A, Mohanram H, Domadia PN, Bhattacharjya S. (2009) Designed b-Boomerang Antiendotoxic and Antimicrobial Peptides: Structures and Activities in Lipopolysaccharide. J. Biol. Chem., 284(33), 21991-2004. (Selected for “Papers of the Week”) (http://www.jbc.org/content/284/33/21991/suppl/DC1/-/2).

14. Bhunia A, Ramamoorthy A, Bhattacharjya S. (2009), Helical Hairpin Structure of a Potent Antimicrobial Peptide MSI-594 in Lipopolysaccharide Micelles by NMR. Chemistry: A European Journal, 15 (9), 2036-40.

13. Bhunia A, Tang XY, Mohanram H, Tan SM, Bhattacharjya S. (2009), NMR Solution Conformations and Interactions of Integrin aLb2 Cytoplasmic Tails. J. Biol.Chem. 284(6), 3873-84.

12. Bhunia A, Mohanram H, Bhattacharjya S. (2009), Lipopolysaccharide bound structures of the active fragments of fowlicidin-1, a cathelicidin family of antimicrobial and antiendotoxic peptide from chicken, determined by transferred nuclear overhauser effect spectroscopy. Biopolymers, 92(1), 9-22. (Selected for cover page).

11. Bhunia A, Domadia PN, Mohanram H, Bhattacharjya S. (2009), NMR structural studies of the Ste11 SAM domain in the dodecyl phosphocholine micelle. Proteins: Structure, Function and Bioinformatics, 74(2), 328-43.

2008

10. Bhunia A, Schwardt O, Gäje H, Gao GP, Kelm S, Benie AJ, Hricovini M, Peters T, Ernst B. (2008), Consistent bioactive conformation of the Neu5Ac-a-(2®3)Gal epitope upon lectin binding. ChemBioChem, 9(18), 2941-5.

9. Bhunia A, Chua GL, Domadia PN, Warshakoon H, Cromer JR, David SA, Bhattacharjya S. (2008), Interactions of a designed peptide with lipopolysaccharide: Bound conformation and anti-endotoxic activity. Biochem. Biophys. Res. Commun., 369, 853-7.

8. Domadia PN, Bhunia A, Sivaraman J, Swarup S, Dasgupta D. (2008), Berberine targets assembly of Escherichia coli cell division protein FtsZ. Biochemistry, 47, 3225-34.

7. Bhunia A, Domadia PN, Xu X, Gingras R, Ni F, Bhattacharjya S. (2008), Equilibrium unfolding of the dimeric SAM domain of MAPKKK Ste11 from the budding yeast: role of the interfacial residues in structural stability and binding. Biochemistry, 47, 651-9.

2007

6. Domadia PN, Bhunia A, Swarup S, Sivaraman J, Dasgupta D. (2007), Inhibition of bacterial cell division protein FtsZ by cinnamaldehyde. Biochem. Pharmacol., 74, 831-40.

5. Bhunia A, Domadia PN, Bhattacharjya S. (2007), Structural and thermodynamic analyses of the interaction between melittin and lipopolysaccharide. Biochim. Biophys. Acta, 1768, 3282-91.

4. Bhattacharjya S, Domadia PN, Bhunia A, Malladi S, David SA. (2007), High-resolution solution structure of a designed peptide bound to lipopolysaccharide: transferred nuclear Overhauser effects, micelle selectivity, and anti-endotoxic activity. Biochemistry, 46, 5864-74.

2006 and before

3. Zhang YH, Bhunia A, Wan KF, Lee MC, Chan SL, Yu VC, Mok YK. (2006), Chelerythrine and sanguinarine dock at distinct sites on BclXL that are not the classic BH3 binding cleft. J. Mol. Biol., 364, 536-49.

2. Bhunia A, Jayalakshmi V, Benie AJ, Schuster O, Kelm S, Rama Krishna N, Peters T. (2004), Saturation transfer difference NMR and computational modeling of a sialoadhesin-sialyl lactose complex. Carbohydr. Res., 339, 259-67 (Most cited paper award from Elsevier publishers).

1. Bhunia A, Durani S, Wangikar PP. (2001), Horseradish peroxidase catalyzed degradation of industrially important dyes. Biotechnol. Bioeng., 72, 562-7.