Gafni Ari

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Ari Gafni

Ari Gafni.png

Professor of Biophysics and of Biological Chemistry, The University of Michigan.

Ph.D. in Chemical Physics, with special distinction, 1973, from The Weizmann Institute of Science, Israel

Positions

  • 1973-1975 Research Associate, Biology, Johns Hopkins University, Baltimore, MD.
  • 1975-1977 Intermediate Scientist, Department of Chemical Physics, Weizmann Institute of Science, Israel.
  • 1977-1982 Senior Scientist, Dept Chemical Physics, The Weizmann Institute of Science, Rehovot, Israel.
  • 1982-1983 Visiting Scholar, Molecular Biology Institute, UCLA.
  • 1982-1984 Associate Professor of Chemical Physics, The Weizmann Institute of Science.
  • 1983-1991 Associate Research Scientist, Institute of Gerontology and Associate Professor of Biological Chemistry, University of Michigan, Ann Arbor, Michigan.
  • 1989-1992 Editorial Board, Journal of Gerontology, Biological Sciences.
  • 1991-present Senior Research Scientist, Institute of Gerontology and Professor of Biological Chemistry, University of Michigan, Ann Arbor, Michigan.
  • 1995- Member, National Scientific Advisory Board, The American Federation for Aging Research.
  • 1996-2004 Editorial Board, Journal of Fluorescence.
  • 1999 Member, Biol. Sciences Section, Fellowship Committee, Gerontological Society of America.
  • 1998-2000 Director, Institute of Gerontology, University of Michigan, Ann Arbor, Michigan.
  • 2002-2006 Contributing Editor, Science of Aging Knowledge Environment.
  • 2006-2008 Chair, Biological Fluorescence Subgroup, The Biophysical Society.
  • 2007-present Professor of Biophysics, University of Michigan.
  • 2010- Editorial Board, Journal of Experimental Pharmacology.
  • 2011- Editorial Board, Journal of Biophysical Chemistry.

Honors and Awards

  • 1972 The Landau Award, Feinberg Graduate School, The Weizmann Institute of Science.
  • 1973-1975 U.S. State Department post-doctoral training fellowship.
  • 1978-1983 The Henri Glasberg Career Development Chair in Physical Biochemistry.
  • 1982-1983 American Heart Association Senior Investigatorship.
  • 1992- Fellow, The Gerontological Society of America.
  • 1998 Inducted - Society of Scholars, Johns Hopkins University.
  • 1998- Founding Member, the Society of Fluorescence.
  • 2001 Distinguished Director Award, University of Michigan, 2001

Research Interests

My PhD training in chemical physics, followed by postdoctoral training in research on biological systems, has prepared me for a career in biophysics. I have used this expertise to pursue and lead research that focused on macromolecular behavior as well as on methodology development. As a member, and later director, of the Institute of Gerontology at the University of Michigan I was directing projects that aimed to address problems in the basic biology of aging and of aging associated diseases. Recent research in my laboratory has focused on studies of macromolecular interactions, protein folding and misfolding, and on the development of optical spectroscopic methodologies that are effective for these studies.We used these methodologies, for example, to image and follow catalytic cycles of several flavoenzymes. A major current effort in my laboratory is the characterization of the molecular origin of the cytotoxicity of the amyloid beta peptide (Aβ) associated with Alzheimer’s disease. Single molecule imaging and tracking is applied to identify the peptide oligomeric species that interfere with neuronal function and understand the underlying molecular mechanisms of the neurotoxicity. The biophysical tools we have developed allow us to address the molecular pathology involved in Alzheimer’s disease at an unprecedented level of detail and to identify the agents that feature in this pathology. Some of the results of these studies are presented in the publications listed below.

Selected Peer Reviewed Publications

  • Pattaramanon, N, Sangha, N and Gafni, A: The carboxy-terminal domain of HSF1 is intrinsically unstructured and can be induced to fold. Biochemistry 2007; 46, 3405-3415. PMID: 17323918
  • Brender, JR, Lee, EL, Cavitt, MA, Gafni, A, Steel, DG and Ramamoorthy, A: Amyloid fiber formation andmembrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes related peptide. J. Am. Chem. Soc. 2008, 130, 6424-6429. PMID: 18444645
  • Shi, J., Gafni, A. and Steel, DG: Application of single molecule spectroscopy in studies of enzyme kinetics and mechanisms. Meth. Enzymol. 2008; 450, 129-157.PMID: 19152859
  • Wong, P, Schauerte, JA, Wisser, KC, Ding, H, Lee, E, Steel, DG and Gafni, A: Amyloid-β membrane binding and permeabilization are distinct processes influenced by membrane charge and fluidity. J. Mol. Biol., 2009,386, 81-96. PMID: 19111557.
  • Tapley, T.L., Körner, J.L., Barge, M.T., Hupfeld, J., Schauerte, J.A., Gafni, A., Jakob, U. and Bardwell, J.C.A. A Functional Role for Protein Disorder: Rapid Activation and Substrate Binding in the Miniature Chaperone HdeA. Proc. Natl. Acad. Sci. USA. 2009; 106, 5557-5562. PMCID:PMC2660062.
  • Ding, H., Wong, PT, Lee, EL, Gafni, A. and Steel, DG: Determination of the oligomer size of amyloidogenic beta-amyloid(1-40) by single-molecule spectroscopy. Biophys. J. 2009; 97, 912-921.PMCID:PMC2718150.
  • Schauerte, JA, Wong, PT, Wisser, KC, Steel, DG and Gafni, A: Distinct Classes of Amyloid Pores Formed by Aβ1-40 on Lipid Bilayers are revealed by Simultaneous Single Molecule Fluorescence and ConductivityMeasurements. Biochemistry2010; 49, 3031-3039. PMC2862386.
  • Brender JR, Lee EL, Hartman K, Wong PT, Ramamoorthy A, Steel DG, Gafni A: Biphasic effects of insulin on islet amyloid polypeptide membrane disruption. Biophys. J. 100 2011; 685-692. PMC3030259
  • Wijeyesakere SJ, Gafni A andRaghavan M:Calreticulin is a thermostable protein with distinct structural responses to different divalent cation environments. J. Biol. Chem. 2011, 286:8771-85. PMC3058961.
  • Johnson, R. D., J. A. Schauerte, K. C. Wisser, A. Gafni, and D. G. Steel: Direct observation of single amyloid-beta(1-40) oligomers on live cells: binding and growth at physiological concentrations. PLoS One 6(8), 2011: e23970. PMC3162019.
  • Ding, H, Schauerte, JA, Steel, DG and Gafni, A: β-amyloid(1-40) Peptide Interacting with Supported Anionic Lipid Membranes: A Single Molecule Study. Biophys. J., 103 (2012) 1500-1509.PMC3471456.
  • Johnson, R. D, Schauerte, JA, Chang, CC, Wisser, KC, Althaus, JC, Carruthers, CJL, Sutton, MA and Gafni, A.: Single-Molecule Imaging Reveals Ab42:Ab40 Ratio-Dependent Oligomer Growth on Neuronal Processes. Biophys. J., 104 (2013) 1-10. PMC3576537.
  • Chang, CC, Althaus, JC, Carruthers, CJL, Sutton, MA, Steel, DG and Gafni, A.: Synergistic Interactions between Alzheimer’s Aβ40 and Aβ42 on the Surface of Primary Neurons Revealed by Single Molecule Microscopy. PLoS One DOI: 10.1371/journal.pone.0082139, 2013. PMC3847093.
  • Johnson, R.D, Steel, DG, and Gafni, A.: Structural Evolution and Membrane Interactions of Alzheimer’s Amyloid-Beta Peptide Oligomers: New Knowledge from Single-Molecule Fluorescence Studies. Protein Sci., 23 (2014) 869-883. PMC4088971
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