Basir Ahmad
Reader 'F'
Basir Ahmad |


  • PhD (Biotechnology) Aligarh Muslim University (April 2008), Specializations: Molecular Biophysics and Biophysical Chemistry
  • MSc (Biotechnology) Aligarh Muslim University (July 2002), Specializations: Protein Chemistry
  • BSc Honors (Chemistry) Aligarh Muslim University (July1999)


  • Reader-F : UM- DAE Centre for Excellence in Basic Sciences (August 2013-Present)
  • Visiting Scientist : UM- DAE Centre for Excellence in Basic Sciences (April 2013-July 2013)
  • Research Associate: UM- DAE Centre for Excellence in Basic Sciences (June 2012-March 2013)
  • Visiting Research Associate: Michigan State University, East Lansing, MI, USA (January 2010-Febraury 2012)
  • Postdoctoral Fellow: University of Florence, Italy (November 2007-December 2009)


  • Protein folding and stability
  • Protein misfolding and aggregation
  • Drug development against aggregation based diseases
  • Drug-protein Interaction Studies

Selected Publications:

  • Borana MS, Mishra P, Pissurlenkar RR, Hosur RV, Ahmad B* (2014) Curcumin and Kaempferol Prevent Lysozyme Fibril Formation by Modulating Aggregation Kinetic Parameters. Biochim Biophys Acta. 2014 Jan 24. pii: S1570-9639(14)00012-0. doi: 10.1016/j.bbapap.2014.01.009.
  • Kamtekar N, Pandey A, Agrawal N, Pissurlenkar  RRS, Borana B,  Ahmad B* (2013) Interaction of Multimicrobial Synthetic Inhibitor 1,2-Bis(2-Benzimidazolyl)-1,2-Ethanediol with Serum Albumin: Spectroscopic and Computational Studies. PLoS ONE 8(1) e3872
  • Ahmad B, Chen Y, Lapidus LJ (2012) Aggregation of α-Synuclein is Kinetically Controlled by Intramolecular Diffusion. Proc.Nat.Acad.Sci.USA 109(7):2336-2341.
  • Ahmad B, Lapidus LJ (20012) Curcumin Prevents Aggregation in α-synuclein by Increasing Intramolecular Diffusion J. Biol. Chem. 287(12):9193-9199.
  • Ahmad B, Vigliotta I, Tatini F, Campioni S, Mannini B, Winkelmann J, Tiribilli B, Chiti F. (2011). The induction of {alpha}-helical structure in partially unfolded HypF-N does not affect its aggregation propensity. Protein Eng. Des. Sel. 24(7):553-563.
  • Ahmad B, Winkelmann J, Tiribilli B, Chiti F.(2010). Searching for conditions to form stable protein oligomers with amyloid-like characteristics: The unexplored basic pH. Biochim. Biophys. Acta. 1804, 223-234.
  • Fatima S, Ahmad B, Khan RH. (2007) Native-like tertiary structure in the Mucor miehei lipase molten globule state obtained at low pH. IUBMB Life. 59, 179-186
  • Ahmad B, Shamim TA, Haq SK, Khan RH. (2007). Identification and characterization of functional intermediates of stem bromelain during urea and guanidine hydrochloride unfolding. J. Biochem. 141, 251-259.
  • Ahmad B, Khan RH. (2006). Studies on the acid unfolded and molten globule states of catalytically active stem bromelain: a comparison with catalytically inactive form. J. Biochem. 140, 501-508.
  • Ahmad B, Parveen S, Khan RH. (2006) Effect of albumin conformation on the binding of ciprofloxacin to human serum albumin: a novel approach directly assigning binding site. Biomacromolecules. 7, 1350-1456.
  • Ahmad B, Ansari MA, Sen P, Khan RH. (2006). Low versus high molecular weight poly(ethylene glycol)-induced states of stem bromelain at low pH: stabilization of molten globule and unfolded states. Biopolymers. 81, 350-359.
  • Ahmad B, Ankita, Khan RH. (2005). Urea induced unfolding of F isomer of human serum albumin: a case study using multiple probes. Arch. Biochem. Biophys. 437, 159-167.
  • Ahmad B, Ahmed MZ, Haq SK, Khan RH. (2005). Guanidine hydrochloride denaturation of human serum albumin originates by local unfolding of some stable loops in domain III. Biochim. Biophys. Acta. 1750, 93-102.
  • Ahmad B, Khan MK, Haq SK, Khan RH. (2004). Intermediate formation at lower urea concentration in 'B' isomer of human serum albumin: a case study using domain specific ligands. Biochem. Biophys. Res. Commun. 314, 166-73.


UM-DAE Centre for Excellence in Basic Sciences
Health Centre, University of Mumbai,
Vidyanagari Campus, Kalina, Santacruz (East), Mumbai 400098, India.
Phone: 91-22-26524983
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About Us

CBS was set up by the Department of Atomic Energy and the University of Mumbai in 2007. CBS offers a 5 year integrated MSc program in Basic Sciences, with undergraduate teaching embedded in a postgraduate and research environment, for students who have completed 10+2 schooling or its equivalent.