SHARMISTHA SINHA, Ph.D.
Assistant Professor, Institute of Nanoscience and Technology, Mohali, Punjab, India
Institute of Nano Science and Technology
Habitat Centre, Phase- 10, Sector- 64
Mohali, Punjab - 160062
Phone Numbers : +91-172-2210073/75
Fax Number: +91-172-2211074
E-mail ID: sinhas [at] inst.ac. in
Website: Sinha Lab
Tel: 0172 - 2210075
1. Bacterial Microcompartments as Nanoreactors.
2. Protein nanostructures from bacterial microcompartments
3.Functional amyloid as model for studying amyloid aggregation and disaggregation.
Specialties: Protein Chemistry; Protein nanostructures; Amyloidogenic Proteins; Bacterial Genetics; Imaging techniques such as AFM,TEM;Cell Biology and Tissue culture techniques
Awards and Distinction:
♦ Recipient of the INSA Medal for Young Scientist 2008, Indian National Science Academy, Government of India.
Degrees:
Ph.D., Biophysics, Indian Institute of Science (Bangalore, India)
- 2002 M.Sc. Physical Chemistry; Grade: First Class, Institution: Department of Chemistry, Burdwan University, Burdwan, INDIA 2000
- B.Sc. Chemistry, Physics, Mathematics. Grade: First Class, Institution: SikshaBhavan, VisvaBharati University, Santiniketan, INDIA
Experience
March 2014 – Present Ajithgarh (Mohali)
February 2010 – October 2013 (3 years 9 months)
Postdoctoral Scientist, Mentoring Graduate and Undergradutae Student
April 2008 – February 2010 (1 year 11 months)
- Past Advisors:
- Research:
Engineering Protein Nanostructures from Bacterial Microcompartments
Bioremediation and waste water management
Targeting and delivery of biomolecules
- Other Experience:2006-2013Post doctoral Fellow
- Honors:2008INSA, Young Scientist Medal
- Awards and Distinctions
- a) Recipient of the 2012 Committee for Professional Opportunities for Women Travel Award to attend Biophysical Society 56th Annual Meeting.
- b) Recipient of the INSA Medal for Young Scientist 2008, Indian National Science Academy, Government of India.
- c) Recipient of Junior Research Fellowship, Council of Scientific and Industrial Research (CSIR), Government of India, 2002-2004 and its Senior Research Fellowship from Aug 2004.
- d) Recipient of Merit Scholarship of VisvaBharati University 1997-1999.
- CV:CV-Sinha-2014.pdf
- file:///C:/Users/anthonyc/Downloads/CV-Sinha-2014.pdf
- sharmisthas@gmail.com
Areas of Research Interest
1. Biomaterials based on Prokaryotic Protein Assemblies
2. Biosensors and Bio-targeting
3. Drug design for Protein misfolding diseases 4. Ligand-Protein interactions
5. Protein Structure-Function relationship
6. Genetic engineering of prokaryotic macromolecular assemblies
Research Achievements
1. Microcompartments and Ordered Protein Sheets in Bacteria: Biomedical and Biotechnological Implications (Feb 2010-Present): Bacterial microcompartments (BMC) are 50-100 nm sized all protein organelles that optimize several conditional metabolic reactions in bacteria. Using genetic engineering, electron microscopy, fluorescence spectroscopy and crystallographic structure determination I explored the crucial factors for stability and integrity of such an architecture. These studies have far reaching implications in the field of drug targeting, delivery, bio nano-reactors and bio-fuel production.
2. Drug Design (May 2008-Jan 2010): This project involved understanding the nano structures involved in nucleation of protein aggregation followed by targeting such structures for development of process specific drug for protein aggregation. I used spectroscopic, physiological, structural biological (NMR and MS), and animal model for development of such a drug. This work received a lot of media attention.
3. Molecular Basis of Cataract in Danish Dementia (Nov 2006-Apr 2008): Danish dementia is associated with an early age cataract. I explored the interactions of Danish dementia peptides with the eye lens crystalins and demonstrated using biophysical, cell biological and animal models that crystallins loose their chaperone properties upon interacting with these peptides. I was awarded the INSA Medal for Young Scientist 2008 for this work.
4. Glycosylation in Legume Lectins (Aug 2002-Nov 2006): Using legume lectins as paradigm and with the help of biophysical, biochemical and bioinformatics tools I was able to show the importance of glycosylation in the stability and unfolding pathway of oligomeric proteins.
Patents
37. Sinha,S., P. Talbiersky, A. Lomakin, F.-G. Klärner, T. Schrader, S. Frautschy, and G. Bitan. International Patent Application No. PCT/US2010/026419, titled "Molecular Tweezers for the Treatment of AmyloidRelated Diseases". (Pending)
38. T Schrader, K Hochdorffer, J Marz-Berberich, L Nagel-Steger, G Bitan, S Sinha. International Patent Application No. PCT
Recent Publications
1. S Sinha, S Cheng, YW Sung, DE McNamara, MR Sawaya, TO Yeates, TA Bobik. Alanine scanning mutagenesis identifies an asparagine-arginine-lysine triad essential to assembly of the shell of the pdu microcompartment. J Mol Biol. 2014;426(12):2328-45.
2. S. Cheng, Fan, C.,S Sinha, T A Bobik The PduQ enzyme is an alcohol dehydrogenase used to recycle NAD+ internally within the Pdumicrocompartment of Salmonella enterica. PlosOne20127(10):e47144.
3. Fan, C.,S. Cheng, S Sinha, T A Bobik. Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments.Proc. Natl. Acad. Sc. USA2012109(37):14995-5000.
4. Sinha, S., Lopes, DHJ. And Bitan G, A key role for lysine residues in amyloid beta-protein folding, assembly, and toxicity. ACS Chemical Neuroscience.2012.3 (6): 473–481.
5. S. Sinha, Z. Du, P. Maiti, F.-G. Klärner, T. Schrader, C. Wang, and G. Bitan, Comparison of three amyloid assembly inhibitors – the sugar scyllo-inositol, the polyphenol epigallocatechingallate, and the molecular tweezers CLR01. ACS Chemical Neuroscience.2012 3 (6):451–458.
6. S. Prabhudesai,* S. Sinha*, A. Attar, A. Kotagiri, A.G. Fitzmaurice, R. Lakshmanan, M.I. Ivanova, J.A. Loo, F-G Klärner, T. Schrader, M. Stahl, G. Bitan, JM Bronstein. A Novel “Molecular Tweezer” Inhibitor of α-Synuclein Neurotoxicity in vitro and in vivo.Neurotherapeutics.2011 9(2):464-76(* equal contribution)
7. Sinha, S, S. Cheng, C. Fan, T. Bobik. The PduM protein is a structural component of the microcompartments involved in coenzyme B12-dependent 1,2-propanediol degradation by Salmonella. J. Bacteriol.194(8):1912-8.
8. Sinha, S., D.H. Lopes, Z. Du, E.S. Pang, A. Shanmugam, A. Lomakin, P. Talbiersky, A. Tennstaedt, K. McDaniel, R. Bakshi, P.Y. Kuo, M. Ehrmann, G.B. Benedek, J.A. Loo, F.G. Klarner, T. Schrader, C. Wang, and G. Bitan, Lysine-specific molecular tweezers are broad-spectrum inhibitors of assembly and toxicity of amyloid proteins. J. Am. Chem. Soc., 2011. 133(42): 16958-69.
9. Hochdorffer, K., J. Marz-Berberich, L. Nagel-Steger, M. Epple, W. Meyer-Zaika, A.H. Horn, H. Sticht, S. Sinha, G. Bitan, and T. Schrader, Rational design of beta-sheet ligands against Ab42-induced toxicity. J. Am. Chem. Soc., 2011. 133(12): 4348-58.
10. Cheng, S., S. Sinha, C. Fan, Y. Liu, and T.A. Bobik, Genetic analysis of the protein shell of the microcompartments involved in coenzyme B12-dependent 1,2-propanediol degradation by Salmonella. J. Bacteriol., 2011. 193(6): p. 1385-92
11. S. Sinha, Z. Du, P. Maiti, F.-G. Klärner, T. Schrader, C. Wang, and G. Bitan, Comparison of three amyloid assembly inhibitors – the sugar scyllo-inositol, the polyphenol epigallocatechingallate, and the molecular tweezers CLR01. ACS Chemical Neuroscience.2012 3 (6):451–458.
12. S. Prabhudesai,* S. Sinha*, A. Attar, A. Kotagiri, A.G. Fitzmaurice, R. Lakshmanan, M.I. Ivanova, J.A. Loo, F-G Klärner, T. Schrader, M. Stahl, G. Bitan, JM Bronstein. A Novel “Molecular Tweezer” Inhibitor of α-Synuclein Neurotoxicity in vitro and in vivo.Neurotherapeutics.2011 9(2):464-76(* equal contribution)
13.
Surolia, I*.,
S. Sinha*, D.P. Sarkar, P.Y. Reddy, G.B. Reddy, and A. Surolia, Concurrence of Danish dementia and cataract: insights from the interactions of dementia associated peptides with eye lens alpha-crystallin.
PLoS One, 2008.
3(8): p. e2927.
(*equal contribution)
14.
Sinha, S. and A. Surolia, Attributes of glycosylation in the establishment of the unfolding pathway of soybean agglutinin.
Biophys. J., 2007.
92(1): p. 208-16.
15.
Sinha, S., G. Gupta, M. Vijayan, and A. Surolia, Subunit assembly of plant lectins.
Curr. Opin. Struct. Biol., 2007.
17(5): p. 498-505.
16.
Sinha, S. and A. Surolia, Oligomerization endows enormous stability to soybean agglutinin: a comparison of the stability of monomer and tetramer of soybean agglutinin.
Biophys. J., 2005.
88(6): p. 4243-51.
17.
Sinha, S., N. Mitra, G. Kumar, K. Bajaj, and A. Surolia, Unfolding studies on soybean agglutinin and concanavalin a tetramers: a comparative account.
Biophys. J., 2005.
88(2): p. 1300-10.
Book Chapters:
♦ Amyloids and Protein Aggregation—Analytical Methods. Li H, F Rahimi, K Murakami, SSinha, P Maiti, G Bitan.Encyclopedia of Analytical Chemistry. 2009
♦ Application of Photochemical Cross-linking to the Study of Oligomerization of Amyloidogenic Proteins. Lopes DHJ, S Sinha, C Rosensweig, G Bitan. Methods Mol Biol. 849:11-21.2012
Causes Sharmistha cares about:
- Education
- Environment
- Health
- Science and Technology
-
Positions held at Padakshep:
Core group member and volunteer.
BURDWAN, INDIA
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