Sandip K Nandi
Total years in experience: 5
Papers published in journals: 20
Papers presented in conferences: 9
Academic Background (Degrees, University Name & Year of Passing):
2016 - Ph.D., IIT Bhubaneswar, India
2010 - M.Sc., Indian School of Mines Dhanbad, India
2008 – B.Sc. (Hons.), Burdwan University, Burdwan, India
2016-2021: Postdoctoral Fellow at School of Medicine, University of Colorado, Anschutz Medical Campus, Aurora, Colorado, USA
Honours and Achievements:
2019 Awarded Best Poster at the School of Pharmacy Research Retreat, Breckenridge, Colorado, USA
2019 Awarded 3rd prize in Poster presentation competition at Postdoc Research Day, University of Colorado Denver, USA
2015 Awarded 1st prize in Poster presentation competition at Research Scholar’s day celebration, IIT Bhubaneswar
2014 Awarded “Royal Society of Chemistry Best Poster Award”, at ACBIR 2014, organised by Department of Chemistry, NIT Rourkela
2013 Awarded 3rd prize in Poster presentation competition at Research Scholar’s day celebration, IIT Bhubaneswar
2012 Awarded “Dr. D. S. Bhakuni Award” for best oral presentation at 49th Annual Convention of Chemists – 2012 of Indian Chemical Society held at NITTTR, Bhopal
2011 Awarded 2nd prize in Poster presentation competition at Research Scholar’s day celebration, IIT Bhubaneswar
2010 Qualified GATE (Chemistry)
2009 Recipient of “Tarubala & Sushil Kumar Dasgupta Memorial Award” for proficiency in B.Sc. examination-2008 from Dept. of Chemistry, B. B. College, Asansol
2001-02 Secured 2nd position in Academics at school
2001-02 Secured 3rd prize in Mental Maths competition at school
He worked on structural and functional properties of small heat shock proteins. He used various biochemical and biophysical techniques in his studies. During his doctoral research, he investigated the molecular chaperone function of a small heat shock protein, HSP18, of Mycobacterium leprae. He demonstrated that HSP18 exists as an oligomeric protein and functions as a molecular chaperone. Biophysical studies demonstrated that this protein prevents enzyme inactivation under stress conditions, reduces redox stress, helps other proteins to refold and prevent thermal killing of E. coli cells, and thereby helps the pathogen to survive in host species.
During his postdoctoral research, he worked on lens proteins, specifically, on α-crystallins. He investigated the role of protein acylation on the structure and function α-crystallin. He showed that protein acylation by acetylation and succinylation enhances the chaperone activity of α-crystallin. He determined the role of sirtuins (SIRTs) in lens aging and cataract formation. This study showed that SIRT3 and SIRT5 are present in lenses and they regulate acylation of proteins. In addition, he studied the role of glycation-mediated cross-linking on the chaperone-substrate complexes of human lens proteins. This project involved testing the role of advanced glycation end products (AGEs) in lens resilience. He demonstrated that that the α-crystallin-client proteins are susceptible for AGE-mediated cross-linking and his study suggested that such cross-linking could play a role in lens aging and cataract formation. Additionally, he worked on a project to develop Carboxitin, which when delivered into lenses increases the GSH levels and traps dicarbonyl compounds. This reduces the AGE-mediated lens stiffness and thereby can delay the onset of presbyopia in human.
Interests: Cataract, presbyopia, tuberculosis, heat shock proteins, protein posttranslational modifications, drug delivery
1. Nandi SK, Rankenberg J, Rakete S, Nahomi RB, Glomb MA, Linetsky MD, Nagaraj RH. Glycation-mediated protein crosslinking and stiffening in mouse lenses are inhibited by carboxitin in vitro. Glycoconj J. 2020 Nov 27. PMID: 33245448.
2. Nandi SK, Rankenberg J, Glomb MA, Nagaraj RH. Transient elevation of temperature promotes cross-linking of a-crystallin-client proteins through formation of advanced glycation endproducts: A potential role in presbyopia and cataracts. Biochem Biophys Res Commun. 2020 Oct 17. PMID: 33081971.
3. Nandi SK, Nahomi RB, Rankenberg J, Glomb MA, Nagaraj RH. Glycation-mediated inter-protein cross-linking is promoted by chaperone-client complexes of a-crystallin: Implications for lens aging and presbyopia. J Biol Chem. 2020 Apr 24; 295(17):5701-5716. PMID: 32184356.
4. Nandi SK, Chakraborty A, Panda AK, Biswas A. M. leprae HSP18 suppresses copper (II) mediated ROS generation: Effect of redox stress on its structure and function. Int J Biol Macromol. 2020 Mar 01; 146:648-660. PMID: 31883890.
5. Nandi SK, Nahomi RB, Harris PS, Michel CR, Fritz KS, Nagaraj RH. The absence of SIRT3 and SIRT5 promotes the acetylation of lens proteins and improves the chaperone activity of a-crystallin in mouse lenses. Exp Eye Res. 2019 05; 182:1-9. PMID: 30849386.
6. Nandi SK, Rakete S, Nahomi RB, Michel C, Dunbar A, Fritz KS, Nagaraj RH. Succinylation Is a Gain-of-Function Modification in Human Lens aB-Crystallin. Biochemistry. 2019 03 05; 58(9):1260-1274. PMID: 30758948.
7. Nandi SK, Chakraborty A, Panda AK, Kar RK, Bhunia A, Biswas A. Evidences for zinc (II) and copper (II) ion interactions with Mycobacterium leprae HSP18: Effect on its structure and chaperone function. J Inorg Biochem. 2018 11; 188:62-75. PMID: 30121399.
8. Nandi SK, Chakraborty A, Panda AK, Biswas A. Conformational perturbation, hydrophobic interactions and oligomeric association are responsible for the enhanced chaperone function of Mycobacterium leprae HSP18 under pre-thermal condition. RSC Advances. 2016; 6(67):62146–62156.
Projects or Ph.D.s guided: None
Books Published: None
Member (Annual), Association for Research in Vision and Ophthalmology (ARVO)
Member (Annual), International Maillard Reaction Society (IMARS)
Personal interests: I love music and try my hands on various cuisines