プロフィール詳細

プロジェクトを作成

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Dr. Sudeshna G.に依頼

India

Biochemist and Analytical Scientist with 12+ years in research; Scientific consultant with 3+ years in industry

プロフィール概要

I am a biochemist. I did my PhD from IIT Kharagpur in protein aggregation and its relation to diseases, understanding the mechanistic pathway and its possible prevention using therapeutics. Further, I went for a postdoc at Technion, Israel and worked with protein crystallography to understand the structure, function, and activity of various proteins. I received prestigious fellowships (CSIR, Lady Davis, Israel Higher Council) during my studies. I have received Inspire faculty fellowship and grant to carry out my independent research in Alzheimer's disease. Currently, I am working as a consultant (Sr Associate Researcher) at Hypsous to help them analyse data or information, literature, building and mapping project outline as per clients requirement where my skills are useful. Key Qualifications  Over 14 years of research expertise in protein and peptide aggregation, as well as small molecule interactions, with a strong focus on spectroscopy and microscopy techniques  Extensive experience in the expression, purification, and crystallization of heat-shock and cyanobacterial proteins  PhD in Biophysical Chemistry, with a focus on interdisciplinary scientific research Experience Scientific Consultant at Hypsous (Freelance/Remote) March 2022-Present  Provide scientific guidance and advice on ongoing research across diverse fields  Assist in identifying opportunities for new product development  Offer technical direction to professionals, helping them achieve their objectives Inspire Faculty at IIT Kanpur March 2017-Feb 2023  Led studies on amyloid beta peptide aggregation kinetics and prevention, utilizing spectroscopic and microscopic techniques, with publications as lead and corresponding author  Authored a comprehensive review article on amyloid beta oligomers, focusing on their formation, pathological relevance, and prevention strategies, also published as lead and corresponding author  Successfully established small-scale research facilities, overseeing the procurement and management of materials for wet-lab research Postdoctoral Researcher at Technion June 2014-June 2016  Conducted extensive research on the expression, purification, and crystallization of small heat-shock proteins from T. vulcanus, published as the first author  Optimized the growth conditions for various cyanobacterial strains and carried out protein purification using ultracentrifugation methods Project Name: Amyloid beta peptide aggregation and possible prevention Role: Lead researcher, corresponding author, handled all the wet-lab research experiments Tools Used: Fluorescence, CD, Raman, Microscopy (SEM, TEM), Molecular docking Project Description: The DST-funded Inspire project was focused on understanding the aggregation mechanism of amyloid beta peptides and their link with Alzheimer's disease. We have chosen the 25-35 beta peptide fragment and monitored its aggregation kinetics using spectroscopic and microscopic techniques. We have also studied the effect of carvedilol, a known beta blocker, on the aggregation kinetics to determine if it can prevent or inhibit the aggregation process. Outcome of the Project: The 25-35 beta peptide fragment forms striated and twisted fibrils. Fluorescence and CD confirm the aggregation, and microscopic images show the morphological aspects. The beta peptide fragment undergoes helical to beta-sheet formation during aggregation, which was interrupted by carvedilol, and thus, inhibition of aggregation occurs. The molecular docking study suggested that Ile 31 and Ile 32 are the core residues responsible for aggregation and interaction with the carbazole moiety of carvedilol. Our study was in-depth and provided a deep insight into the aggregation mechanism and prevention aspect of Alzheimer's Project Name: A study on amyloid beta oligomers Role: lead and corresponding author Project Description: A detailed literature review has been prepared on various aspects of amyloid beta oligomers which are considered to be the most neurotoxic species responsible for Alzheimer's pathogenesis. Several studies and their outcome have been discussed. Also an interesting hypothesis have been proposed which describes how the best inhibitor for amyloid oligomers can be designed using an optimized control strategy. Outcome of the Project: The review has been well put together and covers various facets of amyloid oligomer formation. The review provides intricate information and guides the researcher in designing wet lab research experiments. Postdoctoral Researcher at Technion June 2014-June 2016  Conducted extensive research on the expression, purification, and crystallization of small heat-shock proteins from T. vulcanus, published as the first author  Optimized the growth conditions for various cyanobacterial strains and carried out protein purification using ultracentrifugation methods Project Name: Structure, function, and activity of heat shock proteins Role as a Researcher: lead author, carried out all the biophysical experiments in vitro (Fluorescence, CD, Chaperone activity assay), Overexpressed and purified the protein using chromatographic techniques, Set up crystallization Tools Used: Fluorescence, CD, UV, protein overexpression and purification using affinity chromatography and size-exclusion chromatography Project Description: We have determined the structure, function, and activity of a small heat-shock protein from a thermophilic cyanobacteria T vulcanus. We have used biophysical, biochemical, spectroscopic, microscopic, and crystallographic techniques to unravel the structure, function, and activity of the heat- shock protein. Protein overexpression was carried out in E. coli BL21 strain and purification was performed using Ni-chromatography followed by size-exclusion chromatography. The purity was checked with SDS- PAGE and MALDI-TOF. Small heat shock protein was soluble in 2 M urea in Tris buffer pH 8. Concentrated and purified protein was subjected to crystallization and crystals were obtained in PEG MME 550. Diffraction data was collected at the ESRF synchrotron facility and data sets obtained were analyzed using standard software packages. Outcome of the Project: Detailed analysis was performed to get in-depth insights. The crystallographic analysis indicates that the crystal structure of heat shock protein contains 0.6 M urea where urea molecules interact with the protein directly and indirectly and are thus responsible for the onset of denaturation. The unique interactions lead to the loss of secondary structure elements while preserving the tertiary structure. Our study provides an understanding of the loss of local interactions, however, the long-range interactions were maintained and therefore the data obtained was difficult to refine to the very highest possibility. We have verified our results using biophysical and biochemical techniques ensuring that even though there is an initiation of denaturation in the presence of urea in the crystal structure, it retains its functional secondary structure in solution and the crystal form. Project Name: Isolation, purification, and characterization of cyanobacterial proteins Role as a Researcher: Isolation, purification and characterization of cyanobacterial proteins, set up crystallization Tools Used: Sucrose gradient method for protein isolation, Purification using Ion-exchange chromatography, and size exclusion chromatography Project Description: The goal was to obtain diffraction-quality crystals of allophycocyanin and phycocyanin proteins from thermophilic cyanobacteria. We performed a sucrose-based gradient method to isolate the targeted proteins and further carried out dialysis followed by column chromatographic methods to purify them. Outcome of the Project: The purified proteins were set up for crystallization, and crystals were sent to the Imperial College of London for further high-end spectroscopic analysis.

専門分野

• ☆ Physical Chemistry
• ☆ Biochemistry
• ☆ Biochemical Assays
• ☆ Structural Biology
• ☆ Enzyme Activity Assays
• ☆ Binding Assays
• ☆ Biophysics
• ☆ Biotechnology & Bioengineering
• ☆ Recombinant Protein Expression
• ☆ Microscopy
• ☆ Light Microscopy
• ☆ Electron Microscopy
• ☆ Fluorescence Microscopy
• ☆ Scanning Probe Microscopy
• ☆ Food Chemistry
• ☆ Plant-Based Protein

サービス

• Writing
• Research
• Consulting
• Data & AI

Writing Technical Writing

Research Technology Scouting, Fact Checking

Consulting Scientific and Technical Consulting

Data & AI Image Processing, Image Analysis, Data Visualization

職務経験

Sr Associate Researcher

Hypsous

3月 2022 - 現在

DST-Inspire Faculty

Indian Institute of Technology Kanpur

3月 2017 - 現在

Postdoctoral Researcher

Technion Israel Institute of Technology

6月 2014 - 6月 2016

学歴

PhD (Chemistry)

Indian Institute of Technology Kharagpur

8月 2008 - 2月 2014

MSc

Presidency College, University of Calcutta

4月 2006 - 3月 2008

BSc (Hons)

Presidency College, University of Calcutta

4月 2003 - 3月 2006

認定資格

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出版物

JOURNAL ARTICLE

(2021). Carvedilol inhibits Aβ_25-35 fibrillation by intervening the early stage helical intermediate formation: A biophysical investigation . International journal of biological macromolecules.

Ghosh, S., Salama, F., Dines, M., Lahav, A., Adir, N.(2019). Biophysical and structural characterization of the small heat shock protein HspA from Thermosynechococcus vulcanus in 2 M urea . Biochimica et Biophysica Acta - Proteins and Proteomics. 1867. (4). Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 442-452.

Dinda, A.K., Chattaraj, S., Ghosh, S., Tripathy, D.R., Dasgupta, S.(2016). DNA melting properties of the dityrosine cross-linked dimer of Ribonuclease A . Journal of Photochemistry and Photobiology B: Biology. 162. Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 535-543.

Tripathy, D.R., Pandey, N.K., Dinda, A.K., Ghosh, S., Singha Roy, A., Dasgupta, S.(2015). An insight into the ribonucleolytic and antiangiogenic activity of buffalo lactoferrin . Journal of Biomolecular Structure and Dynamics. 33. (1). Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 184-195.

Ghosh, S., Pandey, N.K., Banerjee, P., Chaudhury, K., Nagy, N.V., Dasgupta, S.(2015). Copper(II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions . Journal of Biomolecular Structure and Dynamics. 33. (5). Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 991-1007.

Pandey, N.K., Ghosh, S., Tripathy, D.R., Dasgupta, S.(2015). Effect of temperature and solvent on fibrillation of human serum albumin . Protein and Peptide Letters. 22. (2). Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 112-118.

Ghosh, S., Pandey, N.K., Bhattacharya, S., Roy, A., Nagy, N.V., Dasgupta, S.(2015). Evidence of two oxidation states of copper during aggregation of hen egg white lysozyme (HEWL) . International Journal of Biological Macromolecules. 76. Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 1-9.

Pandey, N.K., Mitra, S., Chakraborty, M., Ghosh, S., Sen, S., Dasgupta, S., DasGupta, S.(2014). Disruption of human serum albumin fibrils by a static electric field . Journal of Physics D: Applied Physics. 47. (30).

Ghosh, S., Pandey, N.K., Dasgupta, S.(2014). Crowded milieu prevents fibrillation of hen egg white lysozyme with retention of enzymatic activity . Journal of Photochemistry and Photobiology B: Biology. 138. Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 8-16.

Pandey, N.K., Ghosh, S., Nagy, N.V., Dasgupta, S.(2014). Fibrillation of human serum albumin shows nonspecific coordination on stoichiometric increment of Copper(II) . Journal of Biomolecular Structure and Dynamics. 32. (9). Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 1366-1378.

Ghosh, S., Pandey, N.K., Sen, S., Tripathy, D.R., Dasgupta, S.(2013). Binding of hen egg white lysozyme fibrils with nucleic acids . Journal of Photochemistry and Photobiology B: Biology. 127. Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 52-60.

Bhattacharya, S., Ghosh, S., Pandey, N.K., Chaudhury, S., Dasgupta, S., Roy, A.(2013). Distribution of protein ramachandran psi (ψ) angle using non-resonance visible raman scattering measurements . Journal of Physical Chemistry B. 117. (45). Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 13993-14000.

Pandey, N.K., Ghosh, S., Dasgupta, S.(2013). Effect of surfactants on preformed fibrils of human serum albumin . International Journal of Biological Macromolecules. 59. Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 39-45.

Ghosh, S., Pandey, N.K., Singha Roy, A., Tripathy, D.R., Dinda, A.K., Dasgupta, S.(2013). Prolonged Glycation of Hen Egg White Lysozyme Generates Non Amyloidal Structures . PLoS ONE. 8. (9).

Pandey, N.K., Ghosh, S., Dasgupta, S.(2013). Fructose restrains fibrillogenesis in human serum albumin . International Journal of Biological Macromolecules. 61. Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 424-432.

Bhattacharya, S., Ghosh, S., Dasgupta, S., Roy, A.(2013). Structural differences between native Hen egg white lysozyme and its fibrils under different environmental conditions . Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. 114. Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 368-376.

Ghosh, S., Pandey, N.K., Dasgupta, S.(2013). (-)-Epicatechin gallate prevents alkali-salt mediated fibrillogenesis of hen egg white lysozyme . International Journal of Biological Macromolecules. 54. (1). Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 90-98.

Ghosh, S., Pandey, N.K., Bhattacharya, S., Roy, A., Dasgupta, S.(2012). Fibrillation of hen egg white lysozyme triggers reduction of copper(II) . International Journal of Biological Macromolecules. 51. (1-2). Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 1-6.

Pandey, N.K., Ghosh, S., Dasgupta, S., Pandey, N.K., Ghosh, S., Dasgupta, S.(2010). Fibrillation in human serum albumin is enhanced in the presence of copper(II) . Journal of Physical Chemistry B. 114. (31). Microsoft.AspNetCore.Mvc.Localization.LocalizedHtmlString 10228-10233.