Tej P. Singh

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Tej Pal Singh
TPSingh.jpg
Born1944
NationalityIndian
CitizenshipIndia
Alma materIndian Institute of Science, Bangalore
Known forProtein Structure Determination, Peptide Design, Drug Design
AwardsGoyal Prize 2010 for Life Sciences
Distinguished Biotechnology Research Professor (DBT) (2009)
Distinguished Biotechnologist (DBT) (2006)
GN Ramachandran Gold Medal CSIR)
Scientific career
FieldsRational structure based Drug Design
InstitutionsAll India Institute of Medical Sciences

Tej Pal Singh (born 1944) is an Indian biophysicist known for his work in the fields of rational structure-based drug design, structural biology of proteins and X-ray crystallography.[1] He has played an active role in the development of drug design in the fields of antibacterial therapeutics,[2][3][4][5][6] tuberculosis,[7][6][8] inflammation,[9][10] cancer[11][12] and gastropathy.[10][13]

He is first Indian to receive all the six Ramachandran awards of the country.[14] He is a fellow of six academies, namely, the Third World Academy of Sciences, Indian National Science Academy, National Academy of Sciences, Indian Academy of Sciences, Alexander von Humboldt Foundation and Biotech Research Society of India.[15]

Education[edit]

Tej obtained his master's degree in science from the University of Allahabad. He started his research career in 1971 as a graduate student at the Indian Institute of Science, Bangalore. He obtained his Ph.D. degree in the mid-1970s working on the crystal structure determinations and design of anti-inflammatory analgesics for new drug discovery. [1]. Before going for his bachelor's degree in Science in Allahabad University, Tej Pal Singh has studied in his neighbourhood village school i.e. Kisan Intermediate College Deorhi-Wajidpur (District-Amroha UP) and later Government Intermediate College (GIC) in Amroha (UP).

Professional career[edit]

Soon after obtaining his Ph.D. degree, Tej worked for a year as a lecturer at the University of Indore. He then spent more than two years (1978–1980) as an Alexander von Humboldt / Max-Planck, post doctoral fellow in the German laboratory of Professor Robert Huber, who later received the Nobel Prize. After his return to India he worked as a reader at Sardar Patel University (1980–83) and an additional professor (1984–85) in the Department of Biophysics at the All India Institute of Medical Sciences, New Delhi. He was appointed professor and head of the department in 1986 [2] [3]

Contributions in protein structural biology[edit]

The three-dimensional structures of various proteins including lactoperoxidase,[16] peptidoglycan recognition protein, lactoferrin[17][18][19] from several species, ribosome inactivating proteins,[20] bifunctional inhibitor proteins from plant seeds and various serine proteases and their inhibitors have been determined by his group. The elaborate structural studies of proteins from several important systems as potential drug targets such as phospholipase A2, cyclooxygenase, lipoxygenase, endothelin receptor, endothelin converting enzyme, breast cancer regression proteins and matrix metanosomal proteins as well as their complexes with natural and designed synthetic ligands have been carried out. He had developed the rules of peptide design with alpha, beta – dehydro – amino acids through extensive studies using syntheses, and X-ray and NMR structure determinations. These design rules are being exploited for making specific peptides to act as tight inhibitors of target enzymes and potent antagonists of target receptors for eventually leading to useful therapeutic agents.

He initiated a new programme on Clinical Proteomics at the All India Institute of Medical Sciences in which it is intended to characterize all the proteins that are expressed during various patho/physiological conditions. The newly identified proteins will either be useful as biomarkers or they may be associated with the progression of diseases making them important targets for drug design.

Awards and honors[edit]

Tej is a fellow of the Third World Academy of Sciences, Indian National Science Academy, National Academy of Sciences Indian Academy of Sciences, Alexander von Humboldt Foundation and Biotech Research Society of India. He has won the Goyal Prize for Life Sciences, Distinguished Biotechnology Research Professor (DBT) (2009), GN Ramachandran Gold Medal for excellence in Science and Technology (CSIR) (2006), Distinguished Biotechnologist (DBT), 2006, JC Bose Memorial Award (2005), Alexander von Humboldt Fellow (1977), Canadian development Agency Award (1999)

References[edit]

  1. ^ "On ResearchGate". 29 January 2018. Retrieved 29 January 2018.
  2. ^ Sharma, Pradeep; Dube, Divya; Sinha, Mau; Yadav, Savita; Kaur, Punit; Sharma, Sujata; Singh, Tej P. (1 January 2013). "Structural insights into the dual strategy of recognition by peptidoglycan recognition protein, PGRP-S: structure of the ternary complex of PGRP-S with lipopolysaccharide and stearic acid". PLOS ONE. 8 (1): e53756. Bibcode:2013PLoSO...853756S. doi:10.1371/journal.pone.0053756. ISSN 1932-6203. PMC 3541179. PMID 23326499.
  3. ^ Singh, Amit Kumar; Singh, Nagendra; Sharma, Sujata; Singh, S. Baskar; Kaur, Punit; Bhushan, A.; Srinivasan, A.; Singh, Tej P. (29 February 2008). "Crystal structure of lactoperoxidase at 2.4 A resolution". Journal of Molecular Biology. 376 (4): 1060–1075. doi:10.1016/j.jmb.2007.12.012. ISSN 1089-8638. PMID 18191143.
  4. ^ Rastogi, Nilisha; Nagpal, Nitish; Alam, Hammad; Pandey, Sadanand; Gautam, Lovely; Sinha, Mau; Shin, Kouichirou; Manzoor, Nikhat; Virdi, Jugsharan S. (1 January 2014). "Preparation and antimicrobial action of three tryptic digested functional molecules of bovine lactoferrin". PLOS ONE. 9 (3): e90011. Bibcode:2014PLoSO...990011R. doi:10.1371/journal.pone.0090011. ISSN 1932-6203. PMC 3940724. PMID 24595088.
  5. ^ Rastogi, Nilisha; Singh, Avinash; Pandey, Sada Nand; Sinha, Mau; Bhushan, Asha; Kaur, Punit; Sharma, Sujata; Singh, Tej P. (1 June 2014). "Structure of the iron-free true C-terminal half of bovine lactoferrin produced by tryptic digestion and its functional significance in the gut". The FEBS Journal. 281 (12): 2871–2882. doi:10.1111/febs.12827. ISSN 1742-4658. PMID 24798798. S2CID 24534041.
  6. ^ a b Singh, Avinash; Gautam, Lovely; Sinha, Mau; Bhushan, Asha; Kaur, Punit; Sharma, Sujata; Singh, T. P. (1 January 2014). "Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Å resolution shows the closed structure of the substrate-binding cleft". FEBS Open Bio. 4: 915–922. doi:10.1016/j.fob.2014.10.010. ISSN 2211-5463. PMC 4226762. PMID 25389518.
  7. ^ Sharma, Pradeep; Yamini, Shavait; Dube, Divya; Singh, Amar; Mal, Gorakh; Pandey, Nisha; Sinha, Mau; Singh, Abhay Kumar; Dey, Sharmistha (1 January 2013). "Structural basis of the binding of fatty acids to peptidoglycan recognition protein, PGRP-S through second binding site". Archives of Biochemistry and Biophysics. 529 (1): 1–10. doi:10.1016/j.abb.2012.11.001. ISSN 1096-0384. PMID 23149273.
  8. ^ Singh, Avinash; Kumar, Ashok; Gautam, Lovely; Sharma, Pradeep; Sinha, Mau; Bhushan, Asha; Kaur, Punit; Sharma, Sujata; Arora, Ashish (1 November 2014). "Structural and binding studies of peptidyl-tRNA hydrolase from Pseudomonas aeruginosa provide a platform for the structure-based inhibitor design against peptidyl-tRNA hydrolase". The Biochemical Journal. 463 (3): 329–337. doi:10.1042/BJ20140631. ISSN 1470-8728. PMID 25101795.
  9. ^ Shukla, Prakash Kumar; Gautam, Lovely; Sinha, Mau; Kaur, Punit; Sharma, Sujata; Singh, Tej P. (1 April 2015). "Structures and binding studies of the complexes of phospholipase A2 with five inhibitors". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854 (4): 269–277. doi:10.1016/j.bbapap.2014.12.017. ISSN 0006-3002. PMID 25541253.
  10. ^ a b Sharma, Pradeep; Dube, Divya; Singh, Amar; Mishra, Biswajit; Singh, Nagendra; Sinha, Mau; Dey, Sharmistha; Kaur, Punit; Mitra, Dipendra K. (6 May 2011). "Structural basis of recognition of pathogen-associated molecular patterns and inhibition of proinflammatory cytokines by camel peptidoglycan recognition protein". The Journal of Biological Chemistry. 286 (18): 16208–16217. doi:10.1074/jbc.M111.228163. ISSN 1083-351X. PMC 3091228. PMID 21454594.
  11. ^ Bilgrami, Sameeta; Yadav, Savita; Kaur, Punit; Sharma, Sujata; Perbandt, Markus; Betzel, Christian; Singh, Tej P. (23 August 2005). "Crystal structure of the disintegrin heterodimer from saw-scaled viper (Echis carinatus) at 1.9 A resolution". Biochemistry. 44 (33): 11058–11066. doi:10.1021/bi050849y. ISSN 0006-2960. PMID 16101289.
  12. ^ Mohanty, Ashok K.; Singh, Garima; Paramasivam, Murugan; Saravanan, Kolandaivelu; Jabeen, Talat; Sharma, Sujata; Yadav, Savita; Kaur, Punit; Kumar, Pravindra (18 April 2003). "Crystal structure of a novel regulatory 40-kDa mammary gland protein (MGP-40) secreted during involution". The Journal of Biological Chemistry. 278 (16): 14451–14460. doi:10.1074/jbc.M208967200. ISSN 0021-9258. PMID 12529329.
  13. ^ Mir, Rafia; Singh, Nagendra; Vikram, Gopalakrishnapillai; Sinha, Mau; Bhushan, Asha; Kaur, Punit; Srinivasan, Alagiri; Sharma, Sujata; Singh, Tej P. (15 August 2010). "Structural and binding studies of C-terminal half (C-lobe) of lactoferrin protein with COX-2-specific non-steroidal anti-inflammatory drugs (NSAIDs)". Archives of Biochemistry and Biophysics. 500 (2): 196–202. doi:10.1016/j.abb.2010.05.026. ISSN 1096-0384. PMID 20515646.
  14. ^ "Prof T P Singh became the first Indian to receive all Ramachandran Awards". biotechexpressmag.com. 19 March 2020. Archived from the original on 6 May 2022. Retrieved 6 May 2022.
  15. ^ "BRSI". www.brsi.in.
  16. ^ Singh, A..; Singh, N.; Sharma, S.; Singh, S.B.; Kaur, P.; Bhushan, A.; Srinivasan, A.; Singh, T.P. (14 December 2007). "Crystal structures of lactoperoxidase at 2.4 A resolution". Journal of Molecular Biology. 376 (4): 1060–1075. doi:10.1016/j.jmb.2007.12.012. PMID 18191143.
  17. ^ Sharma, S.; Jasti, J.; Kumar, J.; Mohanty, A.K.; Singh, T.P. (8 August 2003). "Crystal structure of a proteolytically generated functional monoferric C-lobe of bovine lactoferrin at 1.9A resolution". Journal of Molecular Biology. 331 (2): 485–96. doi:10.1016/s0022-2836(03)00717-4. PMID 12888354.
  18. ^ Khan, J.A.; Kumar, P.; Paramasivam, M.; Yadav, R.S.; Sahani, M.S.; Sharma, S.; Srinivasan, A.; Singh, T.P. (8 June 2001). "Camel lactoferrin, a transferrin-cum-lactoferrin: crystal structure of camel apolactoferrin at 2.6 A resolution and structural basis of its dual role". Journal of Molecular Biology. 309 (3): 751–761. doi:10.1006/jmbi.2001.4692. PMID 11397094.
  19. ^ Mir, R.; Singh, N.; Vikram, G.; Kumar, R.P.; Sinha, M.; Bhushan, A.; Kaur, P.; Srinivasan, A.; Sharma, S.; Singh, T.P. (16 December 2009). "The structural basis for the prevention of nonsteroidal antiinflammatory drug-induced gastrointestinal tract damage by the C-lobe of bovine colostrum lactoferrin". Biophysical Journal. 97 (12): 3178–3186. Bibcode:2009BpJ....97.3178M. doi:10.1016/j.bpj.2009.09.030. PMC 2793366. PMID 20006955.
  20. ^ Kushwaha, G.S.; Pandey, N.; Sinha, M.; Singh, S.B.; Kaur, P.; Sharma, S.; Singh, T.P. (April 2012). "Crystal structures of a type-1 ribosome inactivating protein from Momordica balsamina in the bound and unbound states". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1824 (4): 679–91. doi:10.1016/j.bbapap.2012.02.005. PMID 22361570.

External links[edit]