Anirban Bhunia Assistant Professor  Contact  Office: Annex building, 2nd floor Telephone: +91-33-25693336 E-mail: bhunia@bic.boseinst.ernet.in or anirbanbhunia@gmail.com

Education 

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

Professional Experiences

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 for their 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. Carbohydrate mimic peptide based drug design. 

 Open position: If you are interested for pursuing PhD, please feel free to contact by email. (Click for details)

Publications (* corresponding author)

2013

1. Jana J, Kar RK, Ghosh A, Biswas A, Ghosh S, Bhunia A*, Chatterjee S.*(2013) Human cathelicidin peptide LL37 binds telomeric G-quadruplex. Mol Biosyst. 2013 May 1. [Epub ahead of print]

2012

1. 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.

2. Kar RK, Suryadevara P, Jana J, Bhunia A*, Chatterjee S* (2012) Novel G-quadruplex Stabilizing Agents: In-silico Approach and Dynamics. Journal of Biomolecular Structure and Dynamics (in press).

3. Mohanram H, Nip A, Domadia PN, Bhunia A, Bhattacharjya S. (2012) NMR structure, localization, and vesicle fusion of chikungunya virus fusion Peptide. Biochemistry (in press).

4.  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.

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

2011

1. 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

1. 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. 

2. 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.

3. Bhunia A, Vivekanandan S, Eckert T, Burg-Roderfeld M, Wechselberger R, Romanuka J, Bächle D, Kornilov AV, von der Leith C-W, Barbero JJ, Nifantiev N, Schachner M, Sewald N, Lütteke 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.  

4. 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. 

5. 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. 

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

2009

1. 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). 

2. 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. 

3. 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. 

4. 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). 

5. 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

1. Bhunia A, Schwardt O, Gäthje 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. 

2. 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. 

3. 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. 

4. 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. 

2007

1. 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. 

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

3. 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

1. 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). 

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