Personal Information

Dr. Jay Kant Yadav

Associate Professor and Head
Department of Biotechnology

M.Sc., Ph.D. (Biotechnology)

jaykantyadav@curaj.ac.in

91
  • Structure – Function Relationships of Amyloids: With reference to Alzheimer's disease
  • Molecular Mechanism of Amyloid-Induced Cataract formation
  • Amyloids of Anti-Microbial Peptides

 

Education

  • B.Sc. (Zoology, Botany & Chemistry), First Class, Udai Pratap Autonomous College, Varanasi, Poorvanchal University, U.P., India. 1997-2000​
  • M.Sc. (Biotechnology), First Class, Department of Biotechnology, University of Calicut, Kerala, India, 2000-2002                     
  • Ph.D. (Biotechnology), Department of Protein Chemistry and Technology, CSIR-Central Food Technological Research Institute (University of Mysore), Mysore, India, 2003-2009                     Thesis title: Structure, Function and Stability of α-Amylases in the Presence of Various Co-Solvents.
  • Supervisor: Dr. V. Prakash, Ex-Director CFTRI, Mysore and Distinguished Scientist of CSIR

 Fellowships and Awards

  • CSIR-NET-JRF (Dec. 2002)
  • GATE (Graduate Aptitude Test in Engineering) 2002
  • Recipient of student fellowship sponsored by Dept. of Biotechnology (DBT) Govt. of India during M.Sc. (Biotechnology) programme. (July 2000 – June 2002)
  • Deputed as Inspired Teacher and participated in the meeting ‘In-Residence Programmes of Inspired Teachers’ chaired by President of India at the President House (Rashtrapati Bhawan), New Delhi.  https://en.wikipedia.org/wiki/Inspired_Teacher      
  • Recipient of Carrier Achievement Award presented during 19th World Congress of IUFoST-2018.
  • Champion Award for the Food Sustainability Idea/Concept Development Competition presented at the 21st World Congress of Food Science and Technology at Singapore. (Title: Integration of dairy based protein nanostructures for the management of Alzheimer’s disease),  3rd November 2022                                                                                  

Developing SMART therapeutics for non-invasive treatment of Age-related Cataract in Human Eye

According to World Health Organization (WHO), 90% of blind people live in the developing countries [Fact sheet of WHO, 2013]. Of these, >65% cases of blindness occur due cataract. Blindness has a great impact not only in terms of illness but it also obstructs socio-economic development. WHO survey shows, there is a backlog of 12 million blind eyes in India, of which cataract contributes 80% [Murthy, et al, 2007; Kanagarajan et al, 2011]. At present, there is no effective drug/ molecules available that can stop or delay cataract development. The currently available treatment involves surgical replacement of affected lens by a plastic one. Although, this method has shown encouraging success and acceptability among the people, the affordability of the treatment and management of post-operative complications is a major concern.

The eye lens consists of highly concentrated (up to 400 mg/ml) homogeneous solution of proteins. Crystallins constitute 90% of total lens protein [Bloemendal et al, 2004]. They are generally classified into three types, commonly referred as a-, β-, and g-crystallins. The chaperone activity of the α-crystallins is believed to be essential for the maintenance of lens transparency [Horwitz, 1992; Merck et al, 1993]. They are heteropolymer of two homologous subunits; αA-crystallin and αB-crystallin, in a ratio of 3:1. Both the subunits are stabilized by an inter-subunit bridging via zinc ions. With increasing age or due to some unknown factors aA-crystallins slowly lose their chaperon activity and undergo proteolytic cleavage to release low molecular weight (LMW) peptides (e.g., aA-(66-80), aA-(67-80), aA-(67-75), etc.)  [Santhosh kumar et al, 2008]. These peptides possess high aggregation propensity and form amyloid like fibrillar structures in vitro. Accumulation of these peptides in lens aggravates native a-crystallins aggregation and loss of their chaperon activity. These events ultimately cause deterioration of optical quality of eye lens and lead to development of cataract. Here we propose a research plan to investigate the molecular mechanism of αA-crystallin aggregation induced by its own fragments.  

In order to address the above the major objective of the current proposal is to develop an efficient strategy to disaggregate the crystalline aggregates isolated from cataract human eye lens, which will further lead to development of non-invasive anti-cataract therapy. We assume that deciphering the mechanism of crystallin aggregation will be able to provide a scientific basis for designing potential therapeutic strategies for prevention and treatment of cataract. 

Amyloids of Antimicrobial Peptides: A New Paradigm for Antimicrobial Approaches

Antimicrobial peptides (AMPs) have been isolated and characterized from a wide range of animals, plants and bacterial species and are known to play important roles in the host defence system. With the growing problem of pathogenic organisms which are resistant to conventional antibiotics, AMPs emerge as potential alternatives to the conventional antibiotics due to their unique antimicrobial activity. For examples, AMPs exhibit broad-spectrum activity and they selectively destabilize the physical integrity of the bacterial membrane and therefore are unlikely to induce bacterial resistance. Regardless of these distinct advantages, there are several key challenges still limit their widespread application, including low oral bioavailability due to enzymatic degradation in the gastrointestinal tract. On the other hand, these peptides have unique physicochemical properties, such as self-association and aggregation that give rise to different formulation challenges, particularly with respect to conformational stability. Generally, protein/ peptide aggregation is considered to be a consequence of alteration in secondary and tertiary structure that might be linked to loss or gain of function. Our recent studies suggested that considerable fraction of AMPs sequences registered in antimicrobial database (APD) possess moderate to high aggregation propensity and form fibrillar aggregates under in vitro conditions. These aggregates possess the biophysical properties of classical amyloids. However, the impact of aggregation on antimicrobial activities of AMPs is not yet known. Furthermore, due to the innate amyloidogenic characteristics, the AMPs may undergo rapid aggregation and form a range of conformational variants (e.g., oligomers, protofibrils and fibrils), which might have different structural and functional attributes.

Therefore, we propose a hypothesis that the different conformational states of AMPs aggregates might be associated with diverse biophysical properties and antimicrobial activities. To evaluate this hypothesis the proposed research plan aims to perform in silico comparative analyses of intrinsic aggregation propensity of AMPs listed in the AMP database and to assess the aggregation behavior of selected AMPs under in vitro conditions. Due to their inherent amyloidogenic potential, studies is being carried out to examine whether any conformational variants (e.g., oligomeric, protofibrillar and fibrillar) exist during AMPs aggregation. The outcome of the proposed study would enable development of strategies to stabilize and formulate AMPs high efficacy antimicrobials. 

S. No. Authors Title of Article Journal/Conference Details Journal/Conference Publication Year
1 Malik S and Yadav J. K. Amyloids and amyloid-like protein aggregates in Food System: Challenges and New Perspectives. Current Protein & Peptide Science Journal 2023
2 Jangir N., Bangrawa S., Yadav T., Malik S., Alamri S. A., Galanakis C. M., Singh M., Yadav J. K. Isolation and characterization of amyloid-like protein aggregates from soya beans and effect of low pH and heat-treatment on their stability. Journal of Food Biochemistry, 46(10): 2022, e14369. (IF: 2.72) Journal 2022
3 Malik S., De I., Singh M., Galanakis C.M., Alamri A.S., Yadav J.K. Isolation and characterization of milk-derived amyloid-like protein aggregates (MAPA) from cottage cheese. Food Chemistry, 373: 2022, 131486. (IF: 7.27) Journal 2022
4 Yadav J.K. Structural and functional swapping of amyloidogenic and antimicrobial peptides: Redefining the role of amyloidogenic propensity in disease and host defense. J. Pept. Sci., 28(4): 2021, e3378. (IF: 2.408) Journal 2021
5 Mittal C., Kumari A., De I., Singh M., Harsolia R.S., Yadav J. K. Heat treatment of soluble proteins isolated from human cataract lens leads to the formation of non-fibrillar amyloid-like protein aggregates. Int. J. Biol. Macromol. 2021; 188: 512–522. (IF: 6.953). Journal 2021
6 Verma N, Srivastava S., Malik R., Yadav J. K., Goyal P., Pandey J., Computational investigation for modeling the protein–protein interaction of TasA (28–261)–TapA (33–253): A decisive process in biofilm formation by Bacillus subtilis. J Mol Model., 2020; 26(9): 226 (IF: 1.73) Journal 2020
7 Mittal C., Harsolia R. S., Singh M., Yadav J. K. Disaggregation of amyloid-like protein aggregates isolated from human cataract lens. Indian J. Biochem Biophys. (NISCAIR) 2021; 58: 359-365. (IF: 1.918) Journal 2021
8 Shalini G., Yadav J. K. Aggregation hot spots in the SARS‑CoV‑2 proteome may constitute potential therapeutic targets for the suppression of the viral replication and multiplication. J. Protein Proteom. 2021; 12: 1-13 https://doi.org/10.1007/s42485-021-00057-y Journal 2021
9 Schimansky A., Yadav J. K. Amyloid cross-sequence interaction between Aβ(1‐40) and αA(66–80) in relation to the pathogenesis of cataract. Int. J. Biol. Macromol. 2021; 179: 61-70. (IF: 6.953) Journal 2021
10 Ram L., Mittal C., Harsolia R. S., Yadav J. K. Trehalose inhibits the heat-induced formation of the amyloid-like structure of soluble proteins isolated from human cataract lens. Protein J. 2020 Oct 10. 39(5):509-518 doi: 10.1007/s10930-020-09919-8. (IF: 2.371) Journal 2020
11 Harsolia, R.S., Kanwar, A., Gour, S., Kumar, V.2, Kumar, V.1, Bansal, R., Kumar, S., Singh, M., Yadav J. K. Predicted aggregation-prone region (APR) in βB1-crystallin forms the amyloid-like structure and induces aggregation of soluble proteins isolated from human cataractous eye lens. Int. J. Biol. Macromol. 2020; 163:702-710. (IF: 6.953) Journal 2020
12 Kumar, V., Kumar, P. G., Yadav, J.K. Impact of semen‑derived amyloid (SEVI) on sperm viability and motility: its implication in male reproductive fitness. Eur. Biophys. J. 2019; 48:659–671. (IF: 2.119) Journal 2019
13 Gour, S., Kumar, V., Singh, A., Gadhave, K., Goyal, P., Pandey, J., Giri R., Yadav, J.K. Mammalian antimicrobial peptide Protegrin-4 self assembles and forms amyloid-like aggregates: Assessment of its functional relevance. J. Pept. Sci.  2019; 25(3):e3151. (IF: 1.86) Journal 2019
14 Brünnert D., Shekhawat I., Chahar K. R., Ehrhardt J., Pandey J., Yadav J. K., Zygmunt M., Goyal P., Thrombin stimulates gene expression and secretion of IL-11 via protease-activated receptor-1 and regulates extravillous trophoblast cell migration. J. Reprod. Immunol., 2019; 132: 35-41. (IF: 3.86) Journal 2019
15 Kumar, V., Gour, S., Verma, N., Kumar, S., Gadhave, K., Mishra, PM., Goyal, P., Pandey, J., Giri, R., Yadav, J.K. Pheromone peptide cOB1 from native Enterococcus faecalis forms amyloid-like structures: A new paradigm for peptide pheromones. J. Pept. Sci. 2019; 25(8):e3178. (IF: 1.86) Journal 2019
16 Gour S., Kumar V., Rana M., Yadav J.K. The mechanism of Phosphatidylcholine-induced interference of PAP(248-286) aggregation. J. Pept. Sci. 2019; 25(8):e3157. (IF: 1.86) Journal 2019
17 Röcker A., Roan N.R., Yadav J.K., Fändrich M., Münch J. Structure, function and antagonism of semen amyloids. ACS Chem. Commun. 2018; 54: 5775-5769. (IF: 6.164) Journal 2018
18 Kumar V., Gour S., Peter O. S., Gandhi S., Goyal P., Pandey J., Harsolia R. S., Yadav J. K. Effect of green tea polyphenol epigallocatechin-3-gallate on the aggregation of αA (66-80) peptide, a major fragment of αA-crystallin involved in cataract development. Curr. Eye Res. 2017; 42: 1368-1377. (IF: 1.91) Journal 2017
19 Wulff, M., Baumann, M., Thümmler, A., Yadav, J.K., Heinrich, L., Knüpfer, U.,  Schlenzig, D., Schierhorn, A., Rahfeld, J.,  Horn, U.,  Balbach, J., Demuth, H., Fändrich, M. Enhanced fibril fragmentation of N-terminally truncated and pyroglutamyl-modified Aβ peptide. Angew. Chem. Int. Ed. 2016; 55: 5081–5084. (IF: 16.823) Journal 2016
20 Gour S., Kaushik V., Kumar V., Gaharwar B and Yadav J. K. Targeting the semen derived amyloids to control HIV transmission: perspectives and challenges. J. Protein Proteom. 2016; 7:19-27. Journal 2016
21 Gour,S., Kaushik, V., Kumar, V., Bhat, P., Yadav, S.C., Yadav J.K. Antimicrobial peptide (Cn-AMP2) from liquid endosperm of Cocos nucifera forms amyloid-like fibrillar structure. J. Pept. Sci. 2016; 22: 201-207. (IF: 1.86) Journal 2016
22 Gaharwar, B., Gour, S., Kaushik, V., Kumar, V., Gupta, N., Hause, G., Yadav J.K. Assessment of the effect of macromolecular crowding on aggregation behaviour of a model amyloidogenic peptide. Protein Pept. Lett., 2015, 22: 87-93. (IF: 1.87) Journal 2015
23 Schmidt, M., Rohou, A., Lasker, K., Yadav, J.K., Schiene-Fischer, C., Fändrich, M., Grigorieff, N. Peptide dimer structure in an Aβ(1-42) fibril visualized with cryo-EM. Proc. Natl. Acad. Sci. USA. 2015, 112: 11858-11863. (IF: 12.779) Journal 2015
24 Kumar, S.T., Meinhardt, J., Fuchs, A.K., Aumüller, T., Leppert, J., Büchele, B., Knüpfer, U., Ramachandran, R., Yadav, J.K., Prell, E., Morgado, I., Ohlenschläger, O., Horn, U., Simmet, T., Görlach, M., Fändrich, M. Structure and biomedical applications of amyloid oligomer nanoparticles. ACS Nano, 2014, 8:11042-11052. (IF: 18.027) Journal
25 Usmani, S.M., Zirafi, O., Müller, J.A., Sandi-Monroy, N.L., Yadav, J.K., Meier, C., Weil, T., Roan, N.R., Greene, W.C., Walther, P., Nilsson, K.P., Hammarström, P., Wetzel, R., Pilcher, C.D., Gagsteiger, F., Fändrich, M., Kirchhoff, F., Münch, J. Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen. Nature Communication 2014, 5:3508. (IF: 17.69) Journal 2014
26 Kapfo, W., Grace, S., Chauhan, J.B., Yadav J.K. Effect of non-aqueous solvent on structural stability of α-amylase: a cost-effective prospective for protein stabilization. Process Biochem. 2013, 48: 1025-1030. (IF: 3.757) Journal 2013
27 Li, X., Zhang, X., Ladiwala, A.R., Du, D., Yadav, J.K., Tessier, P., Wright, P., Kelly J., Buxbaum, J. Mechanism of transthyretin inhibition of Aβ aggregation in vitro: insights into in vivo protection. J. Neurosci. 2013, 33: 19423–19433. (IF: 6.709) Journal 2013
28 Guna Sekhar, P.M., Yadav, J.K. Preferential interaction of β-globulin from sesame seeds (Sesamum indicum L.) with cosolvents is accompanied by the protein structural reorganization. Protein Pept. Lett. 2013, 20: 510-520. (IF: 1.87) Journal 2013
29 Haupt C, Leppert J, Rönicke R, Meinhardt J, Yadav, J.K., Ramachandran R, Ohlenschläger O, Reymann KG, Görlach M, Fändrich M. Structural basis of β-amyloid-dependent synaptic dysfunctions. Angew. Chem. Int. Ed. Engl. 2012, 51:1576-1579. (IF:12.089) Journal 2012
30 Yadav, J.K. Macromolecular crowding enhances catalytic efficiency and stability of α-amylase. ISRN Biotechnology, 2013, Article ID 737805, 7 pages. Journal 2013
31 Yadav, J.K. A differential behaviour of α-amylase, in terms of catalytic activity and thermal stability, in response to higher concentration CaCl2. Int. J. Biol. Macromol. 2012, 51:146-152. (IF: 4.05) Journal 2012
32 Yadav J.K., Prakash, V. Stabilization of α-amylase, the key enzyme in carbohydrates properties alterations, at low pH. Int. J. Food Prop. 2011, 14:1182-1196. Journal 2011
33 Yadav J.K., Chandani N, P R Pande Prajakt, Chauhan J.B. Counter effect of sucrose on ethanol-induced aggregation of protein. Protein & Pept. Lett. 2010, 17: 1542-1546. (IF:1.87) Journal 2010
34 Yadav J.K., Prakash V. Thermal stability of α-amylase in aqueous cosolvent systems. J. Biosci., 2009, 34:377-387. (IF:1.67) Journal 2009
35 Yadav J. K. Management of Alzheimer’s disease with Nutraceuticals, In-Nutraceuticals in Brain Health and Beyond (ISBN: 978-0-12-820593-8) Edited by: Dr. Dilip Ghosh, Published by Academic Press Book Chapter 2021
36 Satapathy A. and Yadav J.K. Innovative protein and enzyme engineering processes for the production of biomass hydrolyzing enzymes In- BBB Circular Bioeconomy: Technologies for Biofuels and Biochemicals (ISBN No. Paperback:9780323898553 eBook: 9780323910460) Edited by: Sunita Varjani, Ashok Pandey, Thallada Bhaskar, S.Venkata Mohan, Daniel C.W. Tsang, Published by Elsevier Book Chapter 2021
37 Yadav J.K. Mitigation of inflammation in COVID-19 infection through nutritional management In- Health Hygine, Sanitation and Environment in Pandemic Time (ISBN No. 978-93-5457-589-1, Edited by S R M Pasupuleti, Published by Immortal Publication, India Book Chapter 2022
38 Yadav J.K. Discovery of a fundamental element responsible for transmission of HIV. Vigyan Pragati (ISSN No. 0042-6075), December 2015, Page No. 43. (Originally published in Hindi). Other 2015

Publications 

  1.   Pippal B, Chaudhuri P, Rani K, Yadav J.K., Jain N. Discerning Modulation of α-Synuclein Amyloid Assembly by α-Crystallin. ACS Chem Neurosci. 2023; doi: 10.1021/acschemneuro.3c00052.

  2. Yadav, J. K., Why Millets (Commentary), African Journal Food, Agriculture, Nutrition and Development. 2023, 23 (2); 1-5

  3. Malik S and Yadav J. K. Amyloids and amyloid-like protein aggregates in Food System: Challenges and New Perspectives. Accepted to Current Protein & Peptide Science, 2023. (IF: 3.272) doi: 10.2174/ 1389203724666230104163924.

  4. Jangir N., Bangrawa S., Yadav T., Malik S., Alamri S. A., Galanakis C. M., Singh M., Yadav J. K., Isolation and characterization of amyloid-like protein aggregates from soya beans and effect of low pH and heat-treatment on their stability. Journal of Food Biochemistry, 46(10): 2022, e14369. (IF: 2.72)
  5. Malik S., De I., Singh M., Galanakis C.M., Alamri A.S., Yadav J.K. Isolation and characterisation of milk-derived amyloid-like protein aggregates (MAPA) from cottage cheese. Food Chemistry, 373: 2022, 131486. (IF: 7.27)
  6. Yadav J.K. Structural and functional swapping of amyloidogenic and antimicrobial peptides: Redefining the role of amyloidogenic propensity in disease and host defense. J. Pept. Sci., 28(4): 2021, e3378. (IF: 2.408)
  7. Mittal C., Kumari A., De I., Singh M., Harsolia R.S., Yadav J. K. Heat treatment of soluble proteins isolated from human cataract lens leads to the formation of non-fibrillar amyloid-like protein aggregates. Int. J. Biol. Macromol. 2021; 188: 512–522. (IF: 6.953).
  8. Verma N, Srivastava S., Malik R., Yadav J. K., Goyal P., Pandey J., Computational investigation for modeling the protein–protein interaction of TasA (28–261)–TapA (33–253): A decisive process in biofilm formation by Bacillus subtilis. J Mol Model., 2020; 26(9): 226 (IF: 1.73)
  9. Mittal C., Harsolia R. S., Singh M., Yadav J. K. Disaggregation of amyloid-like protein aggregates isolated from human cataract lens. Indian J. Biochem Biophys. (NISCAIR) 2021; 58: 359-365. (IF: 1.918)
  10. Shalini G., Yadav J. K. Aggregation hot spots in the SARS‑CoV‑2 proteome may constitute potential therapeutic targets for the suppression of the viral replication and multiplication. J. Protein Proteom. 2021; 12: 1-13 https://doi.org/10.1007/s42485-021-00057-y
  11. Schimansky A., Yadav J. K. Amyloid cross-sequence interaction between Aβ(1‐40) and αA(66–80) in relation to the pathogenesis of cataract. Int. J. Biol. Macromol. 2021; 179: 61-70. (IF: 6.953)
  12. Ram L., Mittal C., Harsolia R. S., Yadav J. K. Trehalose inhibits the heat-induced formation of the amyloid-like structure of soluble proteins isolated from human cataract lens. Protein J. 2020 Oct 10. 39(5):509-518 doi: 10.1007/s10930-020-09919-8. (IF: 2.371)
  13. Harsolia, R.S., Kanwar, A., Gour, S., Kumar, V.2, Kumar, V.1, Bansal, R., Kumar, S., Singh, M., Yadav J. K. Predicted aggregation-prone region (APR) in βB1-crystallin forms the amyloid-like structure and induces aggregation of soluble proteins isolated from human cataractous eye lens. Int. J. Biol. Macromol. 2020; 163:702-710. (IF: 6.953)
  14. Kumar, V., Kumar, P. G., Yadav, J.K. Impact of semen‑derived amyloid (SEVI) on sperm viability and motility: its implication in male reproductive fitness. Eur. Biophys. J. 2019; 48:659–671. (IF: 2.119)
  15. Gour, S., Kumar, V., Singh, A., Gadhave, K., Goyal, P., Pandey, J., Giri R., Yadav, J.K. Mammalian antimicrobial peptide Protegrin-4 self assembles and forms amyloid-like aggregates: Assessment of its functional relevance. J. Pept. Sci.  2019; 25(3):e3151. (IF: 1.86)
  16. Brünnert D., Shekhawat I., Chahar K. R., Ehrhardt J., Pandey J., Yadav J. K., Zygmunt M., Goyal P., Thrombin stimulates gene expression and secretion of IL-11 via protease-activated receptor-1 and regulates extravillous trophoblast cell migration. J. Reprod. Immunol., 2019; 132: 35-41. (IF: 3.86)
  17. Kumar, V., Gour, S., Verma, N., Kumar, S., Gadhave, K., Mishra, PM., Goyal, P., Pandey, J., Giri, R., Yadav, J.K. Pheromone peptide cOB1 from native Enterococcus faecalis forms amyloid-like structures: A new paradigm for peptide pheromones. J. Pept. Sci. 2019; 25(8):e3178. (IF: 1.86)
  18. Gour S., Kumar V., Rana M., Yadav J.K. The mechanism of Phosphatidylcholine-induced interference of PAP(248-286) aggregation. J. Pept. Sci. 2019; 25(8):e3157. (IF: 1.86)
  19. Röcker A., Roan N.R., Yadav J.K., Fändrich M., Münch J. Structure, function and antagonism of semen amyloids. ACS Chem. Commun. 2018; 54: 5775-5769. (IF: 6.164)
  20. Kumar V., Gour S., Peter O. S., Gandhi S., Goyal P., Pandey J., Harsolia R. S., Yadav J. K. Effect of green tea polyphenol epigallocatechin-3-gallate on the aggregation of αA (66-80) peptide, a major fragment of αA-crystallin involved in cataract development. Curr. Eye Res. 2017; 42: 1368-1377. (IF: 1.91)
  21. Wulff, M., Baumann, M., Thümmler, A., Yadav, J.K., Heinrich, L., Knüpfer, U.,  Schlenzig, D., Schierhorn, A., Rahfeld, J.,  Horn, U.,  Balbach, J., Demuth, H., Fändrich, M. Enhanced fibril fragmentation of N-terminally truncated and pyroglutamyl-modified Aβ peptide. Angew. Chem. Int. Ed. 2016; 55: 5081–5084. (IF: 16.823)
  22. Gour S., Kaushik V., Kumar V., Gaharwar B and Yadav J. K. Targeting the semen derived amyloids to control HIV transmission: perspectives and challenges. J. Protein Proteom. 2016; 7:19-27.
  23. Gour,S., Kaushik, V., Kumar, V., Bhat, P., Yadav, S.C., Yadav J.K. Antimicrobial peptide (Cn-AMP2) from liquid endosperm of Cocos nucifera forms amyloid-like fibrillar structure. J. Pept. Sci. 2016; 22: 201-207. (IF: 1.86)
  24. Gaharwar, B., Gour, S., Kaushik, V., Kumar, V., Gupta, N., Hause, G., Yadav J.K. Assessment of the effect of macromolecular crowding on aggregation behaviour of a model amyloidogenic peptide. Protein Pept. Lett., 2015, 22: 87-93. (IF: 1.87)
  25. Schmidt, M., Rohou, A., Lasker, K., Yadav, J.K., Schiene-Fischer, C., Fändrich, M., Grigorieff, N. Peptide dimer structure in an Aβ(1-42) fibril visualized with cryo-EM. Proc. Natl. Acad. Sci. USA. 2015, 112: 11858-11863. (IF: 12.779)
  26. Kumar, S.T., Meinhardt, J., Fuchs, A.K., Aumüller, T., Leppert, J., Büchele, B., Knüpfer, U., Ramachandran, R., Yadav, J.K., Prell, E., Morgado, I., Ohlenschläger, O., Horn, U., Simmet, T., Görlach, M., Fändrich, M. Structure and biomedical applications of amyloid oligomer nanoparticles. ACS Nano, 2014, 8:11042-11052. (IF: 18.027)
  27. Usmani, S.M., Zirafi, O., Müller, J.A., Sandi-Monroy, N.L., Yadav, J.K., Meier, C., Weil, T., Roan, N.R., Greene, W.C., Walther, P., Nilsson, K.P., Hammarström, P., Wetzel, R., Pilcher, C.D., Gagsteiger, F., Fändrich, M., Kirchhoff, F., Münch, J. Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen. Nat. Commun. 2014, 5:3508. (IF: 17.69)
  28. Kapfo, W., Grace, S., Chauhan, J.B., Yadav J.K. Effect of non-aqueous solvent on structural stability of α-amylase: a cost-effective prospective for protein stabilization. Process Biochem. 2013, 48: 1025-1030. (IF: 3.757)
  29. Li, X., Zhang, X., Ladiwala, A.R., Du, D., Yadav, J.K., Tessier, P., Wright, P., Kelly J., Buxbaum, J. Mechanism of transthyretin inhibition of Aβ aggregation in vitro: insights into in vivo protection. J. Neurosci. 2013, 33: 19423–19433. (IF: 6.709)
  30. Guna Sekhar, P.M., Yadav, J.K. Preferential interaction of β-globulin from sesame seeds (Sesamum indicum L.) with cosolvents is accompanied by the protein structural reorganization. Protein Pept. Lett. 2013, 20: 510-520. (IF: 1.87)
  31. Haupt C, Leppert J, Rönicke R, Meinhardt J, Yadav, J.K., Ramachandran R, Ohlenschläger O, Reymann KG, Görlach M, Fändrich M. Structural basis of β-amyloid-dependent synaptic dysfunctions. Angew. Chem. Int. Ed. Engl. 2012, 51:1576-1579. (IF:12.089)
  32. Yadav, J.K. Macromolecular crowding enhances catalytic efficiency and stability of α-amylase. ISRN Biotechnology, 2013, Article ID 737805, 7 pages.
  33. Yadav, J.K. A differential behaviour of α-amylase, in terms of catalytic activity and thermal stability, in response to higher concentration CaCl2. Int. J. Biol. Macromol. 2012, 51:146-152. (IF: 4.05)
  34. Yadav J.K., Prakash, V. Stabilization of α-amylase, the key enzyme in carbohydrates properties alterations, at low pH. Int. J. Food Prop. 2011, 14:1182-1196.
  35. Yadav J.K., Chandani N, P R Pande Prajakt, Chauhan J.B. Counter effect of sucrose on ethanol-induced aggregation of protein. Protein & Pept. Lett. 2010, 17: 1542-1546. (IF:1.87)
  36. Yadav J.K., Prakash V. Thermal stability of α-amylase in aqueous cosolvent systems. J. Biosci., 2009, 34:377-387. (IF:1.67)

Book Chapters

  1. Dr. Jay Kant Yadav, Book Chapter: Management of Alzheimer’s disease with Nutraceuticals, In-Nutraceuticals in Brain Health and Beyond (ISBN: 978-0-12-820593-8) Edited by: Dr. Dilip Ghosh, Published by Academic Press
  2. Dr. Aparna Satapathy and Dr. Jay Kant Yadav, Book Chapter:  Innovative protein and enzyme engineering processes for the production of biomass hydrolyzing enzymes, In- BBB Circular Bioeconomy: Technologies for Biofuels and Biochemicals (ISBN No. Paperback:9780323898553 eBook: 9780323910460) Edited by: Sunita Varjani, Ashok Pandey, Thallada Bhaskar, S.Venkata Mohan, Daniel C.W. Tsang, Published by Elsevier
  3. Dr. Jay Kant Yadav, Book Chapter: Mitigation of inflammation in COVID-19 infection through nutritional management, In- Health Hygine, Sanitation and Environment in Pandemic Time (ISBN No. 978-93-5457-589-1, Edited by S R M Pasupuleti, Published by Immortal Publication, India

Articles published in magazines

  1.  Article title: Discovery of a fundamental element responsible for transmission of HIV. Vigyan Pragati (ISSN No. 0042-6075), December 2015, Page No. 43. (Originally published in Hindi).

Principal Investigator

1. Assessment of amyloidogenic propensities of HIV infection enhancing peptide PAP(248-286) under relevant physiological conditions (SB/YS/LS-130/2013) (INR. 19.00/- Lakh). 2013- 2016

Funding agency: Science and Engineering Research Board (SERB-DST), Under Fast Track Young Scientist Scheme, Govt. of India, New Delhi, India.

2. Targeting crystallin-amyloids for the development of non-invasive therapeutic strategy for treatment of age-related cataract(INR. ≈30.00/- Lakh) 2018- 2021

Funding agency: Science and Engineering Research Board (An autonomous body of Department of Science and Technology) (SERB-DST), Govt. of India, New Delhi, India.

Co-Principal Investigator

3. How lysophospholipids (lysophosphatidic acid and sphingosine phosphate) metabolic pathways regulate placental development during pregnancy maintenance (INR. 50.00/- Lakh), 2017-2020

Funding agency: Department of Biotechnology, Ministry of Science and Technology Government of India, New Delhi, India.

Attended

Conferences (Attaendance and Presentations)

  1. Paper presented (Title: Molecular basis of formation of synaptotoxic β-amyloid oligomers) in 82nd Annual meeting of the Society of Biological Chemists (India) & International Conference on Genomes: Mechanism and Function, at University of Hyderabad, Hyderabad, INDIA. (December 2013)
  2. Paper presented (Title: Role of Amyloids in HIV transmission) in 11th BRSI Convention & International Conference on Emerging Trends in Biotechnology, at JNU New Delhi, INDIA.(November 2014)
  3. Paper presented (Title: Effect of N-terminal modifications on Aβ amyloid formation) in National Symposium on Biophysics and Golden Jubilee meeting of the Indian  Biophysical Society at Jamia Millia Islamia, New Delhi, INDIA. (February 2015)
  4. Paper presented (Title: Stabilization of an antimicrobial peptide by exploring their intrinsic biophysical properties) in BITS Conference on Gene and Genome Regulation (BCGGR) at Birla Institute of Technologies and Sciences (BITS), Pilani, Rajasthan, INDIA. (February 2016)
  5. Paper presented (Title: Role of chemical modifications in Alzheimer’s disease) in National Symposium on Emerging Trends in Applied Chemical Sciences (ETACS) at School of Chemical and Pharmaceutical Sciences, Central University of Rajasthan, Ajmer, INDIA. (March 2016)
  6. Paper presented (Title: Role of semen derived amyloids on sperm viability and motility: Relevance in male infertility) in International Conference on Reproductive Health with Emphasis on Strategies for Infertility, Assisted Reproduction and Family Planning & 22nd Annual Meeting of the Indian Society for the Study of Reproduction and Fertility at AIIMS New Delhi. INDIA. (December 2016)
  7. Paper presented (Title: Amyloids of anti-microbial peptides: Amyloids of Antimicrobial Peptides: A New Paradigm towards Development of Peptide-based Antimicrobials) in the International Conference of Intrinsically Disordered Proteins, IISER, Mohali, India. (December 2017)
  8. Paper presented (Title: Amyloidogenic propensity of selected anti-microbial peptides) in 2nd Ulm meeting on ‘Biophysics of Amyloids’, Ulm University, Ulm, Germany. (February 2018)
  9. Paper presented (Title: Amyloids of anti-microbial peptides: A new paradigm of functional amyloids) in Chemistry Department of Technical University of Munich (TUM), Munich Germany. SFB- 1035. (May 2018)
  10. Paper presented (Title: Designing Future Food for Age-Related Human Diseases: With Special Emphasis on Alzheimer’s Diseases) in 19th World Congress of IUFoST-2018, CIDCO Centre, Mumbai, India (October 2018)
  11. Paper presented (Title: Amyloid-like Structures in Surgically Removed Human Cataract Eye Lenses) in 3rd Ulm meeting on ‘Biophysics of Amyloids’, Ulm University, Ulm, Germany. (February 2019)
  12. Invited lecture delivered (Title: Nutritional considerations for healthy aging with special reference to the patients of Alzheimer’s disease) in Food Science Frontier Research Forum, International University Consortium of Food Science and Nutrition, during 17th -19th October 2019, Hangzhou, China. October 2019
  13. Invited lecture delivered (Title: Interfering Amyloid β (Aβ) peptide aggregation to develop therapeutic strategies for the treatment of Alzheimer’s disease) in “Neurocon” held at M.M. University, Mullana-Ambala, Haryana, India, (15-18 November 2019.
  14. Invited lecture delivered (Title: Amyloids of Antimicrobial Peptides: A new paradigm for antimicrobial therapy) in “The Annual BSBE Winter Meeting 2019 “Amyloids:  In Diseases to Promising Materials” held at IIT Kanpur, India, (06th – 7th December 2019).
  15. Delivered an invited lecture in the webinar title: “Development of a peptide-based, rapid, affordable, point-of-care, diagnostic test for COVID-19” at Singapore- Massachusetts Institute of Technology (MIT) Alliance for Research and Technology (SMART) during the DiSTAP Seminar series on 11th June 2020.
  16. Delivered an invited lecture in the webinar title: (Water, Energy and Environment: Challenges & Solutions (WEE-2021) title: “Healthy Aging: Role of Nutrition in Moderating the Molecular Events leading to Alzheimer’s disease” Organized by Department of Chemistry, Institute of Science, GITAM University, Visakhapatnam, India.
  17. Delivered an invited lecture in the GYAN GANGA PROGRAMME, conducted by Commissionerate of College Education Rajasthan, and the Department of Botany, Samrat Prithvi Raj Chauhan Government College, Ajmer, Rajasthan during 1st to 6th February 2021.
  18. Delivered an invited lecture on the topic “Trehalose inhibits the heat-induced formation of the amyloid-like structure of soluble proteins isolated from human cataract lens” in the International Conference on Biotechnology for Sustainable Agriculture, Environment and Health (BSAEH 2021) during 4th to 8th March 2021.
  19. Delivered a plenary lecture in the 1st ECSS Symposium Strengthening Global Food Science and Technology on the topic “The anticipated nutritional and health risks associated with protein-rich foods: with special reference to milk and soy proteins” held during 15-16 September 2021.
  20. Delivered a lecture (Title: Integration of dairy based protein nanostructures for the management of Alzheimer’s disease) for the Food Sustainability Idea/Concept Development Competition in the 21st World Congress of Food Science and Technology at Singapore, and won the CHAMPION award.                                                        

Organized

  1. Organising Secretory of the National Symposium on Good Laboratory Practices & Safety Guidelines (GLPSG-2015) at Central University of Rajasthan, Ajmer, INDIA. (July 2015)
  2. Member of organising committee of Rajasthan Science Congress at Central University of Rajasthan. (October 2018)
  3. Member of organising committee of 19th World Congress of IUFoST2018, CIDCO Centre, Mumbai, India. (October 2018)
Title Attachment File Other Link
Resume PDF icon CV_Dr. Jay Kant Yadav.pdf