Maji, SK

Dr. Samir K. Maji


Phone: +(91-22) 2576 7774
Fax: +(91-22) 2572 7760
E-mail: samirmaji [at]
Location: Room No. 305, BSBE Building
Lab web page

Research Interest

  1. Studying mechanisms of protein mis-folding, aggregation and amyloid formation associated with human neurodegenerative diseases such as Alzheimer’s, Parkinson’s and Prions.
  2. Designing small molecular inhibitors against disease-associated protein oligomerization and amyloid formation.
  3. Understanding the role of amyloid in secretory granules biogenesis in mammalian organs.
  4. De novo design of functional amyloids for drug delivery and tissue engineering

Academic Background

  • 1996: B.Sc (Chemistry) University of Calcutta, Kolkata, WB
  • 1998: M.Sc (Chemistry) University of Calcutta, Kolkata, WB
  • 2002: Ph.D. (Peptide Chemistry) Indian association for The Cultivation of Science, Jadavpur, Kolkata, WB


Biological Thermodynamics and Kinetics, Biophysics Laboratory

Professional Experience

  • Harvard Medical School and BWH , USA
  • University of California, Los Angeles, USA
  • Salk Institute, La jolla, USA
  • ETH Zurich, Switzerland


  • 2013: Young researcher award, Lady Tata memorial Trust
  • 2013: Received International short visit fellowship from Swiss National Science Foundation (SNF)
  • 2013: Selected as a Member of The National Academy of Science, India
  • Young Investigator Travel Award by Protein Society and Finn Wold Travel award
  • 2010: DST-SERC Fast Track for Young Scientists
  • CSIR NET (National Eligibility Test) for Junior Research Fellowship in Chemical Science, Council of Scientific and Industrial Research (CSIR), India.

Selected Publications

  • Narendra Nath Jha, A Anoop, Srivastav Ranganathan, Ganesh M Mohite, Ranjith Padinhateeri, and SK. Maji (2013) Characterization of amyloid formation by glucagon-like peptides: role of basic residues in heparin-mediated aggregation (2013), Biochemistry, 52 (49), pp 8800–8810.
  • Dhiman Ghosh, Mrityunjoy Mondal, Ganesh M. Mohite, Pradeep K. Singh, Priyatosh Ranjan, A. Anoop, Saikat Ghosh, Narendra Nath Jha, Ashutosh Kumar and SK. Maji  (2013) The Parkinsons Disease-Associated H50Q Mutation Accelerates α-Synuclein Aggregation in Vitro, Biochemistry, 52 (40), pp 6925–6927.
  • PK Singh, V Kotia, D Ghosh, GM Mohite, A Kumar and SK Maji (2013) Curcumin modulates a-synuclein aggregation and toxicity, ACS Chem Neurosci, 4(3):393-407.
  • S Ranganathan, PK. Singh, U Singh, PS Singru, R Padinhateeri and SK Maji (2012) Molecular interpretation of ACTH-beta-endorphin coaggregation: relevance to secretory granule biogenesis (2012), Molecular interpretation of ACTH-beta-endorphin coaggregation: relevance to secretory granule biogenesis, PLoS One 7(3):e31924.
  • B Winner*, R Jappelli*, SK. Maji*, PA Desplats, L Boyer, S Aigner,C Hetzer, T Loher, M Vilar, S Campioni, C Tzitzilonis, A Soragni, S Jessberger, H Mira, A Consiglio, E Pham, E Masliah, FH. Gage, and R Riek  (2011) In vivo demonstration that α-synuclein oligomers are toxic, Proc Natl Acad Sci USA 108(10):4194-9 (*equally contributed authors).
  • SK Maji, MH. Perrin, MR Sawaya, S Jessberger, K Vadodaria, RA Rissman, PS Singru, KPR Nilsson, R Simon, D Schubert, D Eisenberg, J Rivier, P Sawchenko, W Vale and R Riek (2009) Functional Amyloids as Natural Storage of Peptide Hormones in Pituitary Secretory Granules, Science 325: 328-332.
  • SK Maji, RRO Loo, M Inayathullah, SM Spring, SS Vollers, MM Condron, G Bitan, JA Loo, and DB Teplow (2009) Amino acid position-specific contributions to amyloid β-protein oligomerization, J Biol Chem. 284: 23580-23591.
  • L Wang, SK Maji, M Sawaya, D Eisenberg and R Riek (2008) Bacterial inclusion bodies contain amyloid-like structure (2008) Bacterial inclusion bodies contain amyloid-like structure, PLoS Biol. 6(8): e195.
  • M Vilar, H-T Chou, T Lührs, SK Maji, D Riek-Loher, R Verel, G Manning, H Stahlberg and R Riek (2008) The Fold of a-Synuclein Fibrils, Proc. Natl. Acad. Sci. USA 105: 8637– 8642.
  • SK Maji, D. Schubert, JE Rivier, C Rivier, S Lee and R Riek (2008) Amyloid as depot for the formulation of long-acting drugs (2008), PLoS Biology, 6(2):e17.