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Sengupta Dr. D.

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Senior Scientist : Physical And Materials Chemistry

+91-20-25902408

d.sengupta@ncl.res.in

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MY AREAS OF EXPERTISE

Bioinformatics, Chemical Biology, Soft Condensed Matter Physics, Structural Biology, Theoretical Chemistry

MY RESEARCH INTERESTS

 

GPCRs

We are currently working on two GPCRs – the serotonin 1A receptor and the ß2 adrenergeic receptor. The main questions we are interested in is how the membrane affects the GPCR organisation and dynamics? Do the membrane components tune or modulate the receptor and its function? What are the energetics and time scales of these interactions?

Antimicrobial Peptide Action

An important focus of our research is the mechanism of action of antimicrobial peptides. We have previously showed the existence of disordered toroidal pores for several of these peptides (See Publications). We have also worked towards developing a framework to effectively combine computer simulations with experimental studies to understand the molecular basis of activity in these peptides. We have studied a cyclic antimicrobial peptide, BPC194, by spectroscopic and computational techniques to infer functionally-important structural features. We have also determined poration propensity and pore size by simulations and successfully related it to measurements from electrophyisiology and fluorescence cross correlation spectroscopy (FCCS) experiments. We are currently collaborating with Dr. S. Kendurkar, NCL, Pune to develop linear antimicrobial peptides for increased potency against plant pathogens.

Caveolin-1 Membrane Interaction

Caveolin-1 (cav-1) is an important membrane protein that plays a vital role in cellular signalling and trafficking by organising membrane domains. The peptide interacts with cholesterol-rich membranes and induces large morphological changes in them forming microdomains such as caveolae. We are currently using coarse-grained molecular dynamics simulations to study the interaction of cav-1 peptides with several model bilayer systems mimicking biological scenarios, such as cholesterol-rich domains, cholesterol-depleted domains and unsaturated lipid domains. We have shown that cholesterol modulates the depth as well as orientation of cav-1 binding to membranes. Furthermore, the presence of cholesterol stabilizes more open conformations of cav-1, and we speculate that the binding modes and open-conformations could be responsible for inducing morphological changes in the bilayer. We have also calculated the partitioning free energy to difference bilayers and show that binding to cholesterol-rich bilayers is more favorable than cholesterol depleted bilayers and the binding to unsaturated bilayers is the least favorable. Binding to cholesterol-rich bilayers also changes the pressure profile of the bilayer to which it is bound and thereby affects the local spontaneous curvature. Our results highlight molecular details of protein-lipid interplay and provide new insights into the effects of cav-1 in tuning the morphology of cholesterol rich membranes.

ACADEMIC QUALIFICATION

 

PhD ,  (2005)

Univ. Of Heidelberg

PROFESSIONAL EXPERIENCE

 

University of Groningen,  Groningen

Postdoctoral Fellow
2006-2011

PUBLICATIONS

 

Thermodynamic and kinetic characterization of transmembrane helix association

Physical Chemistry Chemical Physics  (2015)
Dr. Durba Sengupta, Athale, CA, Deshpande, SA, Gopal, SM, Pawar, AB, Wassenaar, TA

High-Throughput Simulations of Dimer and Trimer Assembly of Membrane Proteins. The DAFT Approach

Journal of Chemical Theory and Computation  (2015)
Dr. Durba Sengupta, Wassenaar, TA, Bockmann, RA, Marrink, SJ, Moussatova, A, Pluhackova, K, Tieleman, DP

AWARDS & HONORS

 

Ramalingaswami Fellowship

2011

PATENTS

 

Novel antimicrobial peptides

WO2016024296 A3
Kendurkar and Sengupta

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