Bitan, Gal, Ph.D.
  • Professor in Residence of Neurology, David Geffen School of Medicine at UCLA

  • Member of Brain Research Institute at UCLA

  • Member of Interdepartmental Ph.D. Program in Neuroscience at UCLA

  • Associate Member of Molecular Biology Institute at UCLA

Bitan, Gal, Ph.D.


Department of Neurology, David Geffen School of Medicine
at University of California at Los Angeles
635 Charles E. Young Drive South
Neuroscience Research Building 1, Room 451
Los Angeles, CA 90095-7334
Tel: (310) 206-2082
Fax: (310) 206-1700
Email: This email address is being protected from spambots. You need JavaScript enabled to view it.



Chemistry and Biochemistry.

Current Research

My laboratory is focused on developing novel, mechanism-based therapy for neurodegenerative diseases, including Alzheimer’s and Parkinson's diseases. We use various types of compounds and methodologies, such as peptides, peptidomimetics, and small molecules. Guiding these efforts are detailed structure–activity relationship studies, structure-based rational design, and structure-guided small scale screening efforts. To prepare and evaluate our compounds, we use techniques ranging from synthetic chemistry, through biochemical and biophysical characterization of the interaction of our compounds with their targets, toxicity assays in cell culture, and testing of lead compounds in animal models. We have identified and currently are developing several lead inhibitors of aberrant protein assembly and toxicity.



  • B.Sc. cum laude The Hebrew University of Jerusalem, Israel. Major: Chemistry and Minor: Biochemistry, 1988.
  • M.Sc. cum laude The Hebrew University of Jerusalem, Israel Organic Chemistry, 1989.
  • Ph.D. summa cum laude The Hebrew University of Jerusalem, Israel Organic Chemistry, 1996.
  • Postdoctoral fellow, Chemistry Department, Clark University, Worcester, MA. Discipline: Structural Biology, 1996-1997. (Advisor: Dale F. Mierke, Ph.D.)
  • Postdoctoral fellow, Division of Bone and Mineral Metabolism, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA. Discipline: Peptide and protein chemistry, 1996-1999. (Advisors: Michael Rosenblatt, M.D. and Michael Chorev, Ph.D.)
  • Postdoctoral fellow, Center for Neurologic Diseases, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA. Discipline: Protein folding and assembly, 1999-2003. (Advisor: David B. Teplow, Ph.D.)


Honors and Awards

1986 Dean’s Scholarship
1987 Dean’s List
1989 Golda Meir Scholarship
2005 Turken Award for Alzheimer's Disease Research



  • X Zheng, D Liu, F-G Klärner, T Schrader, G Bitan, and MT Bowers. Amyloid β-protein Assembly: The Effect of Molecular Tweezers CLR01 and CLR03. J Physical Chemistry B 2015;119:4831-4841. Note: this paper was featured in the ACS Editors' Choice, which are 7 papers chosen each week from among the 50 different journal the American Chemical Society publishes.
  • DHJ Lopes, A Attar, G Nair, EY Hayden, Z Du, K McDaniel, S Dutt, H Bandmann, K Bravo-Rodriguez, S Mittal, F-G Klärner, C Wang, E Sanchez-Garcia, T Schrader, and G Bitan. Molecular tweezers inhibit islet amyloid polypeptide assembly and toxicity by a new mechanism. ACS Chemical Biology 2015;10:1555-1569.
  • G Herzog, MD Shmueli, L Levi, L Engel, E Gazit, F-G Klärner, T Schrader, G Bitan, and D Segal. The Lys-specific molecular tweezer, CLR01, modulates aggregation of mutant p53 DNA binding domain and inhibits its toxicity. Biochemistry 2015;54:3729–3738. Note: this paper was featured in the Spotlights of Chemical Research in Toxicology.
  • E Lump, LM Castellano, C Meier, J Seeliger, N Erwin, B Sperlich, CM Stürzel, S Usmani, RM Hammond, J von Einem, G Gerold, F Kreppel, K Bravo-Rodriguez, T Pietschmann, VM Holmes, D Palesch, O Zirafi, D Weissman, A Sowislok, B Wettig, C Heid, F Kirchhoff, T Weil, F-G Klärner, T Schrader, G Bitan, E Sanchez-Garcia, R Winter, J Shorter, and J Münch. A molecular tweezer antagonizes seminal amyloids and HIV infection. eLife 2015;4:e05397. Note: This paper was covered by press releases in the US and Germany, which were featured on multiple news sites.
  • R Malishev, S Nandi, S Kolusheva, Y Levi-Kalisman, F-G Klärner, T Schrader, G Bitan*, and R Jelinek*. Toxicity inhibitors protect lipid membranes from disruption by Aβ42. ACS Chem. Neurosci. 2015. E-pub ahead of print, DOI: 10.1021/acschemneuro.5b00200. *Co-corresponding authors.
  • R Roychaudhuri, X Zheng, A Lomakin, P Maiti, MM Condron, GB Benedek, G Bitan, MT Bowers, and DB Teplow. Role of species-specific primary structure differences in Aβ42 assembly and neurotoxicity. ACS Chem. Neurosci. 2015. E-pub ahead of print, DOI: 10.1021/acschemneuro.5b00180.
  • S Prabhudesai, S Sinha, A Attar, A Kotagiri, AG Fitzmaurice, R Lakshmanan, MI Ivanova, JA Loo, F-G Klärner, T Schrader, G Bitan*, and J Bronstein*. A Novel "Molecular Tweezer" Inhibitor of α-Synuclein Neurotoxicity in Vitro and in Vivo. Neurotherapeutics 2012;9:464-476. *Co-corresponding authors.
  • P Novick, DHJ Lopes, K Branson, A Esteras-Chopo, IA Graef, G Bitan, and VS Pande. Design of Aβ42 aggregation inhibitors from a predicted structural motif. J. Med. Chem. 2012;55:3002–3010.
  • S Sinha, Z Du, P Maiti, F-G Klärner, T Schrader, C Wang, and G Bitan. Comparison of three amyloid assembly inhibitors – the sugar scyllo-inositol, the polyphenol epigallocatechin gallate, and the molecular tweezer CLR01. ACS Chem. Neurosci. 2012;3:451-458.
  • S Sinha, DHJ Lopes, and G Bitan. A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity. ACS Chem. Neurosci. 2012;3:473-481
  • MM Gessel, C Wu, H Li, G Bitan, J-E Shea, and MT Bowers Aβ(39-42) Modulates Aβ Oligomerization but not Fibril Formation. Biochemistry 2012;51:108-117.
  • H Li, R Zemel, DHJ Lopes, BH Monien, and G Bitan. A two-step strategy for SAR studies of N-methylated Aβ42 C-terminal fragments as Aβ42 toxicity inhibitors. ChemMedChem 2012;7:515-522.
  • G Bitan. Can We Accelerate the Path towards Therapy for Amyloid- Related Diseases? J. Gerontol. Geriatr. Res. 2012;1:e106. doi:10.4172/jggr.1000e106.
  • JM Ringman, AT Fithian, K Gylys, JL Cummings, G Coppola, D Elashoff, D Pratico, J Moskovitz, and G Bitan. Plasma methionine sulfoxide in persons with familial Alzheimer's disease mutations. Dement. Geriatr. Cogn. Disord. 2012;33:219-225.
  • I Solomonov, E Korkotian, B Born, D Kaganovich, Y Feldman, A Bitler, AF Rahimi, H Li, G Bitan, and I Sagi. Zn2+-Aβ complexes form metastable quasi-spherical oligomers that are cytotoxic to cultured hippocampal neurons, J. Biol. Chem. 2012;287:20555-20564.
  • C Ripoli, R Piacentini, E Riccardi, L Leone, G Bitan, and C Grassi. Synaptotoxic effects of different forms of amyloid β-protein in rodent hippocampal neurons and brain slices. Neurobiol. Aging 2012. epub ahead of print. DOI: 10.1016/j.neurobiolaging.2012.06.027.
  • A Attar, C Ripoli, E Riccardi, P Maiti, DD Li Puma, T Liu, J Hayes, MR Jones, K Lichti-Kaiser, F Yang, GD Gale, C&#$5;H Tseng, M Tan, C-W Xie, JL Straudinger, F-G Klärner, T Schrader, SA Frautschy, C Grassi, and G Bitan. Protection of primary neurons and mouse brain from Alzheimer’s pathology by molecular tweezers. Brain 2012. epub ahead of print, DOI: 10.1093/brain/aws289.
  • J Moskovitz, P Maiti, DHJ Lopes, DB Oien, A Attar, T Liu, S Mittal, J Hayes, and G Bitan. Induction of methionine-sulfoxide reductases protects neurons from amyloid β-protein insults in vitro and in vivo. Biochemistry 2011;50:10687–10697.
  • H Li, Z Du, DHJ Lopes, EA Fradinger, C Wang, and G Bitan. C-terminal Tetrapeptides Inhibit Aβ42-induced Neurotoxicity Primarily Through Specific Interaction at the N-terminus of Aβ42. J. Med. Chem. 2011;54:8451-8460.
  • B Urbanc, M Betnel, L Cruz, H Li, EA Fradinger, BH Monien, G Bitan. Structural basis for Aβ1-42 toxicity inhibition by Aβ C-terminal fragments: discrete molecular dynamics study. J Mol Biol. 2011;410(2):316-328.
  • K Hochdörffer, J März-Berberich, L Nagel-Steger, M Epple, W Meyer-Zaika, A Horn, H Sticht, S Sinha, G Bitan, and T Schrader. Rational design of β-sheet ligands against Aβ42-induced toxicity. J. Am. Chem. Soc. 2011;133:4348-4358.
  • P Maiti, R Piacentini, C Ripoli, C Grassi, and G Bitan. Surprising assembly and toxicity behavior of amyloid β-protein oxidized to sulfone. Biochem. J. 2010;433:323-332.
  • H Li, BH Monien, A Lomakin, R Zemel, EA Fradinger, M Tan, SM Spring, B Urbanc, C-W Xie, GB Benedek, and G Bitan. Mechanistic investigation of the inhibition of Aβ42 assembly and neurotoxicity by Aβ42 C-terminal fragments. Biochemistry 2010;49:6358-6364.
  • F Rahimi and G Bitan. Selection of aptamers for amyloid β-protein, the causative agent of Alzheimer's disease. J. Vis. 2010. Exp. 39, doi: 10.3791/1955.
  • P Maiti, A Lomakin, GB Benedek and G Bitan . Despite its role in assembly, methionine 35 is not necessary for amyloid β-protein toxicity. J. Neurochem. 2010;113:1252-1262.
  • B. Urbanc, M Bentel, L. Cruz, G Bitan, and DB Teplow. Elucidation of amyloid β-protein oligomerization mechanisms, J. Am. Chem. Soc. 2010;1312:4266-4280.
  • H Li, BH Monien, EA Fradinger, B Urbanc and G Bitan. Biophysical characterization of Aβ42 C-terminal fragments—inhibitors of Aβ42 neurotoxicity. Biochemistry 2010;49:1259-1267.
  • F Rahimi, K Murakami, JL Summers, C-HB Chen and G Bitan. RNA aptamers generated against oligomeric Aβ40 recognize common amyloid aptatopes with high sensitivity, PLoS ONE, 4, e7694. 2009. doi:10.1371/journal.pone.0007694.
  • SK Maji, RR Ogorzalek Loo, M Inayatullah, SM Spring, SS Vollers, MM Condron, G Bitan, JA Loo, and DB Teplow. Amino acid position-specific contributions to amyloid β-protein oligomerization. J. Biol. Chem. 2009;284:23580-23591.
  • SL Bernstein, NF Dupuis, ND Lazo, T Wyttenbach, MM Condron, G Bitan, DB Teplow, J-E Shea, BT. Ruotolo, CV. Robinson, and MT Bowers. Why Aβ42 is the neurotoxic agent in Alzheimer's disease, not Aβ40: early oligomer studies. Nat. Chem. 2009;1:326-331.
  • C Wu, SL Bernstein, M Murray, MM Condron, G Bitan, MT Bowers, and J-E Shea. Structural characterization of amyloid β-protein C-terminal fragments. J. Mol. Biol. 2009;387:492-501.
  • F Rahimi, P Maiti, and G Bitan. Photo-induced cross-linking of unmodified proteins (PICUP) applied to amyloidogenic peptides. J. Vis. Exp., 2009. doi: 10.3791/1071.
  • EA Fradinger, BH Monien, B Urbanc, A Lomakin, M Tan, H Li, SM Spring, MM Condron, L Cruz, C-W Xie, GB Benedek, and G Bitan. C-terminal peptides co-assemble into Aβ42 oligomers and protect neurons against Aβ42-induced neurotoxicity. Proc. Natl. Acad. Sci. USA 2008;105:14175–14180.
  • MM Condron, BH Monien, and G Bitan. Synthesis and purification of highly hydrophobic peptides derived from the C-terminus of amyloid β-protein. Open Biotechnol, J. 2008;2:87-93.


    • A Attar, D Meral, B Urbanc, and G Bitan. Assembly of amyloid β-protein variants containing familial Alzheimer’s disease-linked amino acid substitutions. In: Bionanoimaging: Protein Misfolding & Aggregation. V Uversky and Y Lyubchenko Eds. Elsevier/Academic Press. 2014:429-442.
    • F Rahimi and G Bitan. Methods for studying and structure–function relationships of non-fibrillar protein assemblies in Alzheimer's disease and related disorders. In: Advances in Alzheimer Research. Vol. 2, DK Lahiri Ed. Bentham Scientific. 2014:291-374.
    • F Rahimi and G Bitan. The structure and function of fibrillar and oligomeric assemblies of amyloidogenic proteins. In: Pre-fibrillar amyloidogenic protein assemblies-common cytotoxins underlying degenerative diseases. F Rahimi and G Bitan, Eds. Springer Science+Media B.V., Dordrecht. 2012;1-36.
    • C Rosensweig, K Ono, K Murakami, D Lowenstein, G Bitan, and DB Teplow. Preparation of stable amyloid β-protein oligomers of defined assembly order. Methods Mol. Biol. 2012;489:23-31.
    • DHJ Lopes, S Sinha, C Rosensweig, and G Bitan. Application of Photochemical Cross-linking to the Study of Oligomerization of Amyloidogenic Proteins. Methods Mol. Biol. 2012;489:11-22.
    • H Li, F Rahimi, K Murakami, P Maiti, S Sinha, and G Bitan. "Amyloids and protein aggregation–analytical methods" In: Encyclopedia of Analytical Chemistry, Ed. R. A. Meyers, John Wiley: Chichester. 2009. DOI: 10.1002/9780470027318.a9038.
    • H Li and G Bitan. SAR and Mechanistic Studies of Tetrapeptide Inhibitors of Aβ42-Induced Neurotoxicity. In: M. Lebl, Ed. Breaking Away: Proceedings of the 21st American Peptide Symposium. 2009;189-190.


  • H Li, BH Monien, A Lomakin, EA Fradinger, SM Spring, B Urbanc, GB Benedek, and G Bitan. Investigation of Aβ42 C-Terminal Fragments as Inhibitors of Aβ42 Assembly and Neurotoxicity. In: M. Lebl, Ed. Breaking Away: Proceedings of the 21st American Peptide Symposium. 2009;187-188.
  • A Shanmugam, BH Monien, and G Bitan. Development in Diagnostic and Therapeutic Strategies for Alzheimer’s Disease. In: Sun M-K, Ed. Research Progress in Alzheimer’s Disease and Dementia. Vol. 3. Nova Science Publisher, Inc. 2008;193-250.
  • G Bitan. Structural study of metastable amyloidogenic protein oligomers by Photo-Induced Cross-linking of Unmodified Proteins (PICUP). Methods Enzymol. 2006;413:217-236.
  • SM Spring, SL Bernstein, ND Lazo, B Urbanc, HE Stanley, MT Bowers, DB Teplow, and G Bitan. Towards Inhibition of Amyloid β-protein Oligomerization. In: Blondelle SE ed. Understanding Biology Using Peptides, American Peptide Society. 2006;515-516.

Research Abstracts


  • Alpha-Synuclein: The Gateway to Parkinsonism, Innsbruck, Austria 2015. F Richter, I Magen, P Lee, S Subramaniam, A Attar, J Hayes, C Zhu¹, N Franich, N Bove, K De La Rosa, J Kwong, G Bitan, and M-F Chesselet. The molecular tweezer CLR01 reduces alpha-synuclein accumulation and improves motor deficits in a mouse model of Parkinson’s disease.
  • The 25&supth; Annual Meeting of the Society for Virology, Bochum, Germany 2015. E Lump, L Castellano, F Kirchhoff, T Schrader, G Bitan, J Shorter and J Münch. The molecular tweezer CLR01 counteracts semen amyloids and HIV infection.
  • The Annual Meeting of the American Society for Biochemistry and Molecular Biology, Boston, MA, USA 2015. G Bitan. Safe Inhibition of Amyloid Proteins Toxicity without Protein Specificity.


  • HIV Research for Prevention, Cape Town, South Africa 2014. E Lump, L Castellano, RM Hammond, K Bravo-Rodriguez, M Holmes, D Weissman, T Schrader, G Bitan, J Shorter, and J Münch. Counteracting semen-mediated enhancement of HIV infection and enveloped virus infection by a lysine-specific molecular tweezer.
  • The 44&supth; Annual Meeting of the Society for Neuroscience, Washington, DC, USA 2014. CV Fontanilla, B Chan, R Rosales, M Chattopadhyay, TT Vu, A Attar, JS Valentine, MH Vidau-Pazos, and G Bitan. Effect of molecular tweezers treatment in a transgenic mouse model of amyotrophic lateral sclerosis.


  • The 23&suprd; Annual Meeting of the Society for Virology, Kiel, Germany 2013. E Varga, L Castellano, C Stürzel T Schrader, G Bitan, J Shorter, and J Münch. CLR01, a molecular tweezer, abrogates semen-mediated enhancement of HIV infection.
  • The 61&supst; ASMS Conference on Mass Spectrometry and Allied Topics, Minneapolis, MN, USA 2013. P Wongkongkathep, S Yin, B Chan, M Chattopadhyay, J Valentine, G Bitan, and JA Loo. Probing Protein-Ligand Interactions Involved in Neurodegenerative Disease Using Native Electrospray Ionization Top-Down Mass Spectrometry.
  • The 43&suprd; Annual Meeting of the Society for Neuroscience, San Diego, CA, USA 2013. F Richter, C Zhu, S Subramaniam, N Franich, N Bove, P Lee, K De La Rosa, J Wong, A Attar, G Bitan and M-F Chesselet. Peripheral and central administration of the molecular tweezer CLR01 shows beneficial effects in mice overexpressing human wildtype alpha-synuclein.
  • The 9&supth; International Symposium on Familial Amyloidotic Polyneuropathy, Rio de Janeiro, Brazil 2013. N Ferreira, A Pereira-Henriques, G Bitan, MJ Saraiva, and MR Almeida. Molecular Tweezers targeting Transthyretin aggregation: therapeutic applications on Familial Amyloidotic Polyneuropathy.


  • Alzheimer's Association International Conference, Vancouver, BC, Canada 2012. A Attar, C Ripoli, E Riccardi, T Liu, MR Jones, F Yang, C-H Tseng, F-G Klärner, T Schrader, SA Frautschy C Grassi, and G Bitan. Lysine-specific molecular tweezers as an Aβ-targeting therapy for Alzheimer's disease protect neurons against Aβ-induced synaptotoxicity and lower Aβ and p-tau load in a mouse model of Alzheimer's disease.
  • Alzheimer's Association International Conference, Vancouver, BC, Canada 2012. S Sinha, DHJ Lopes, Z Du, P Maiti, F-G Klärner, T Schrader, C Wang, and G Bitan. Structural insight into the mechanism of Aβ toxicity and its inhibition by small molecules.
  • The 60th ASMS Conference on Mass Spectrometry and Allied Topics Vancouver, BC, Canada 2012. P Wongkongkathep, J Zhang, G Bitan, F-G Klärner, T Schrader, and JA Loo. Native Protein Surface Mapping using Lysine-specific Compounds and Top-Down Mass Spectrometry.
  • The 9th World Brain Mapping Conference, Toronto, ON, Canada 2012. G Bitan. Aberrant protein self-assembly as a general target for Alzheimer's disease therapy.
  • The 42nd Annual Meeting of the Society for Neuroscience, New Orleans, LA 2012. A Attar and G Bitan. Brain penetration of amyloid assembly and toxicity inhibitor, CLR01, in 12-month- and 24-month-old wild-type and transgenic mice.
  • The 42nd Annual Meeting of the Society for Neuroscience, New Orleans, LA 2012. G Bitan, A Attar, S Sinha, DHJ Lopes, P Maiti, MR Jones, F Yang, SA Frautschy, S Prabhudesai, JM Bronstein, F Richter, M-F Chesselet, Z Du, C Wang, C Ripoli, E Riccardi, C Grassi, F-G Klärner, T Schrader. Molecular tweezers inhibit protein aggregation and toxicity in vitro and in vivo.


  • A Attar and G Bitan. Disrupting Self-Assembly and Toxicity of Amyloidogenic Protein Oligomers by "Molecular Tweezers" – from the Test Tube to Animal Models. Curr. Pharm. Des., 2014;20:2469-2483.
  • A Attar, F Rahimi and G Bitan. Modulators of amyloid protein aggregation and toxicity: EGCG and CLR01. Translational Neurosci., 2013;4:385-409.
  • T Liu and G Bitan. Modulating Self-Assembly of Amyloidogenic Proteins as a Therapeutic Approach for Neurodegenerative Diseases: Strategies and Mechanisms. ChemMedChem. 2012;7:359-374.
  • F Rahimi, A Shuanmugam, and G Bitan. Structure–Function Relationships of Pre-Fibrillar Protein Assemblies in Alzheimer's Disease and Related Disorders. Curr. Alz. Res. 2008;5:319-341.
  • BH Monien, LG Apostolova, and G Bitan. Early diagnostics and therapeutics for Alzheimer’s disease - how early can we get there? Expert Rev. Neurotherapeutics 2006;6:1293-1306.
  • DB Teplow, ND Lazo, G Bitan, SL Bernstein, T Wyttenbach, MT Bowers, A Baumketner, J-E Shea, B Urbanc, L Cruz, J Borreguero, and HE Stanley. Elucidating Amyloid β-protein Folding and Assembly: A Multidisciplinary Approach. Acc. Chem. Res. 2006;39:635-645.
  • G Bitan. Molecular Neurobiology of Alzheimer Disease and Related disorders [Book Review]. Amyloid: J Protein Folding Disord. 2005;12:65-66.
  • G Bitan and DB Teplow. Rapid photochemical cross-linking – a new tool for studies of metastable, amyloidogenic protein assemblies. Acc. Chem. Res. 2004;37:357-364.
  • MD Kirkitadze, G Bitan, and DB Teplow. Paradigm shifts in Alzheimer's and other neurodegenerative diseases: The emerging role of oligomeric assemblies. J. Neurosci. Res. 2002;69:567-577.


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