Basir Ahmad
Reader 'F'
Basir Ahmad | cbs.ac.in

Education:

  • 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)

Positions:

  • 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)

Research:

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

Selected Publications:

  • Sonavane S, Haider SZ, Kumar A, Ahmad B*. Hemin is able to disaggregate lysozyme amyloid fibrils into monomers. Biochim Biophys Acta. 2017 Aug 18. pii:S1570-9639(17)30183-8.
  • Ahmad B*, Borana MS, Chaudhary AP. Understanding curcumin-induced modulation of protein aggregation. Int J Biol Macromol. 2017 Jul;100:89-96.
  • Shukla VK, Singh JS, Vispute N, Ahmad B, Kumar A, Hosur RV. Unfolding of CPR3 Gets Initiated at the Active Site and Proceeds via Two Intermediates. Biophys J. 2017 Feb 28;112(4):605-619.
  • Chaudhary AP, Vispute NH, Shukla VK, Ahmad B*. A comparative study of fibrillation kinetics of two homologous proteins under identical solution condition. Biochimie. 2017 Jan;132:75-84.
  • Muthu SA, Mothi N, Shiriskar SM, Pissurlenkar RR, Kumar A, Ahmad B*. Physical basis for the ofloxacin-induced acceleration of lysozyme aggregation and polymorphism in amyloid fibrils. Arch Biochem Biophys. 2016 Feb 15;592:10-9.
  • Acharya S, Saha S, Ahmad B, Lapidus LJ. Effects of Mutations on the Reconfiguration Rate of α-Synuclein. J Phys Chem B. 2015 Dec 17;119(50):15443-50.
  • Mothi N, Muthu SA, Kale A, Ahmad B*. Curcumin promotes fibril formation in F isomer of human serum albumin via amorphous aggregation. Biophys Chem. 2015 Dec;207:30-9.
  • Ratnaparkhi A, Muthu SA, Shiriskar SM, Pissurlenkar RR, Choudhary S, Ahmad B*. Effects of hesperidin, a flavanone glycoside interaction on the conformation, stability, and aggregation of lysozyme: multispectroscopic and molecular dynamic simulation studies? J Biomol Struct Dyn. 2015 Sep;33(9):1866-79.
  • Shiriskar SM, Agarwal N, Pissurlenkar RR, Ahmad B*. Effects of 2-amino-8-hydroxyquinoline interaction on the conformation of physiological isomers of human serum albumin. Eur Biophys J. 2015 May;44(4):193-205.
  • Ahmad B, Muteeb G, Alam P, Varshney A, Zaidi N, Ishtikhar M, Badr G, Mahmoud MH, Khan RH. Thermal induced unfolding of human serum albumin isomers: assigning residual α helices to domain II. Int J Biol Macromol. 2015 Apr;75:447-52.
  • Naik A, Kambli P, Borana M, Mohanpuria N, Ahmad B, Kelkar-Mane V, Ladiwala U. Attenuation of lysozyme amyloid cytotoxicity by SPION-mediated modulation of amyloid aggregation. Int J Biol Macromol. 2015 Mar;74:439-46.
  • Borana MS, Mishra P, Pissurlenkar RR, Hosur RV, Ahmad B*. Curcumin and kaempferol prevent lysozyme fibril formation by modulating aggregation kinetic parameters. Biochim Biophys Acta. 2014 Mar;1844(3):670-80.
  • Kamtekar N, Pandey A, Agrawal N, Pissurlenkar RR, Borana M, Ahmad B*. Interaction of multimicrobial synthetic inhibitor 1,2-bis(2-benzimidazolyl)-1,2-ethanediol with serum albumin: spectroscopic and computational studies. PLoS One. 2013;8(1):e53499.
  • Ahmad E, Rabbani G, Zaidi N, Ahmad B, Khan RH. Pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin. PLoS One. 2012;7(6):e38372.
  • Ahmad B, Lapidus LJ. Curcumin prevents aggregation in α-synuclein by increasing reconfiguration rate. J Biol Chem. 2012 Mar 16;287(12):9193-9.
  • Ahmad B, Chen Y, Lapidus LJ. Aggregation of α-synuclein is kinetically controlled by intramolecular diffusion. Proc Natl Acad Sci U S A. 2012 Feb 14;109(7):2336-41.
  • Ahmad B, Vigliotta I, Tatini F, Campioni S, Mannini B, Winkelmann J, Tiribilli B, Chiti F. The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity. Protein Eng Des Sel. 2011 Jul;24(7):553-63.
  • Varshney A, Ahmad B, Rabbani G, Kumar V, Yadav S, Khan RH. Acid-induced unfolding of didecameric keyhole limpet hemocyanin: detection and characterizations of decameric and tetrameric intermediate states. Amino Acids. 2010 Aug;39(3):899-910.
  • Ahmad B, Islam Z, Varshney A, Khan RH. Stabilization of folding intermediate states from alkaline induced unfolded state of bovine serum fetuin in trifluoroethanol and acetonitrile. Protein Pept Lett. 2010 May;17(5):660-6.
  • Sen P, Ahmad B, Rabbani G, Khan RH. 2,2,2-Trifluroethanol induces simultaneous increase in alpha-helicity and aggregation in alkaline unfolded state of bovine serum albumin. Int J Biol Macromol. 2010 Mar 1;46(2):250-4.
  • Ahmad B, Winkelmann J, Tiribilli B, Chiti F. Searching for conditions to form stable protein oligomers with amyloid-like characteristics: The unexplored basic pH. Biochim Biophys Acta. 2010 Jan;1804(1):223-34
  • Ahmad B, Rathar GM, Varshney A, Khan RH. pH-Dependent urea-induced unfolding of stem bromelain: unusual stability against urea at neutral pH. Biochemistry (Mosc). 2009 Dec;74(12):1337-43.
  • Sen P, Fatima S, Ahmad B, Khan RH. Interactions of thioflavin T with serum albumins: spectroscopic analyses. Spectrochim Acta A Mol Biomol Spectrosc. 2009 Sep 15;74(1):94-9.
  • Hameed M, Ahmad B, Khan RH, Andrabi KI, Fazili KM. Tertiary butanol induced amyloidogenesis of hen egg white lysozyme (HEWL) is facilitated by aggregation-prone alkali-induced molten globule like conformational state. Protein Pept Lett. 2009;16(1):56-60.
  • Sen P, Ahmad B, Khan RH. Formation of a molten globule like state in bovine serum albumin at alkaline pH. Eur Biophys J. 2008 Oct;37(8):1303-8.
  • Varshney A, Ahmad B, Khan RH. Comparative studies of unfolding and binding of ligands to human serum albumin in the presence of fatty acid: spectroscopic approach. Int J Biol Macromol. 2008 Jun 1;42(5):483-90.
  • Hameed M, Ahmad B, Fazili KM, Andrabi K, Khan RH. Different molten globule-like folding intermediates of hen egg white lysozyme induced by high pH and tertiary butanol. J Biochem. 2007 Apr;141(4):573-83.
  • Fatima S, Ahmad B, Khan RH. Native-like tertiary structure in the Mucor miehei lipase molten globule state obtained at low pH. IUBMB Life. 2007 Mar;59(3):179-86.
  • Ahmad B, Shamim TA, Haq SK, Khan RH. Identification and characterization of functional intermediates of stem bromelain during urea and guanidine hydrochloride unfolding. J Biochem. 2007 Feb;141(2):251-9.
  • Anwar T, Ahmad B, Younus H. Cross-linked stem bromelain: A more stabilized active preparation. Biocatalysis and Biotransformation. 2007, 25, 453-458.
  • Fatima S, Ahmad B, Khan RH. Fluoroalcohols induced unfolding of Succinylated Con A: native like beta-structure in partially folded intermediate and alpha-helix in molten globule like state. Arch Biochem Biophys. 2006 Oct 15;454(2):170-80.
  • Younus H, Jamal S, Ahmad B, Saleemuddin M. Investigation of conformational changes induced by binding of pancreatic RNase to anti-RNase IgG derived Fab monomer using optical procedures. Biochemistry (Mosc). 2006 Feb;71(2):218-21.
  • Ahmad B, Khan RH. Studies on the acid unfolded and molten globule states of catalytically active stem bromelain: a comparison with catalytically inactive form. J Biochem. 2006 Oct;140(4):501-8.
  • Gull N, Kumar S, Ahmad B, Khan RH, Kabir-ud-Din. Influence of urea additives on micellar morphology/protein conformation. Colloids Surf B Biointerfaces. 2006 Aug 1;51(1):10-5.
  • Ahmad B, Ansari MA, Sen P, Khan RH. Low versus high molecular weight poly(ethylene glycol)-induced states of stem bromelain at low pH: stabilization of molten globule and unfolded states. Biopolymers. 2006 Apr 5;81(5):350-9.
  • Ahmad B, Parveen S, Khan RH. Effect of albumin conformation on the binding of ciprofloxacin to human serum albumin: a novel approach directly assigning binding site. Biomacromolecules. 2006 Apr;7(4):1350-6.
  • Ahmad B, Ahmed MZ, Haq SK, Khan RH. Guanidine hydrochloride denaturation of human serum albumin originates by local unfolding of some stable loops in domain III. Biochim Biophys Acta. 2005 Jun 15;1750(1):93-102.
  • Ahmad B, Ankita, Khan RH. Urea induced unfolding of F isomer of human serum albumin: a case study using multiple probes. Arch Biochem Biophys. 2005 May 15;437(2):159-67.
  • Ahmad B, RH Khan Protein Folding: From Hypothesis Driven to Data Mining Pak. J. Biol. Sci, 2005 8(3):487-492.
  • Haq SK, Rasheedi S, Sharma P, Ahmad B, Khan RH. Influence of salts and alcohols on the conformation of partially folded intermediate of stem bromelain at low pH. Int J Biochem Cell Biol. 2005 Feb;37(2):361-74.
  • Ahmad B, Kamal MZ, Khan RH. Alkali-induced conformational transition in different domains of bovine serum albumin. Protein Pept Lett. 2004 Aug;11(4):307-15.
  • Naseem F, Ahmad B, Ashraf MT, Khan RH. Molten globule-like folding intermediate of asialofetuin at acidic pH. Biochim Biophys Acta. 2004 Jun 1;1699(1-2):191-9.
  • Ahmad B, Khan MK, Haq SK, Khan RH. Intermediate formation at lower urea concentration in 'B' isomer of human serum albumin: a case study using domain specific ligands. Biochem Biophys Res Commun. 2004 Jan 30;314(1):166-73.
  • Tayyab S, Ahmad B, Kumar Y, Khan MM. Salt-induced refolding in different domains of partially folded bovine serum albumin. Int J Biol Macromol. 2002 Mar 8;30(1):17-22.

Address

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
Fax: 91-22-26524982
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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.