Past Members

Name Position Research Project Current Position
Robin Roychaudhuri, PhD  Senior Research Associate Structural biology of the amyloid β-protein (Aβ) Research Associate (Faculty of Neuroscience), Johns Hopkins School of Medicine, Department of Neuroscience
Taylor Whitaker, B.S.  Undergraduate Researcher The role of methionine 35 of Aβ42 in structure and aggregation Medical Student, USC
Elisabeth Hodara, B.S.  Undergraduate Researcher Structural elucidation of the Icelandic variant of Aβ42 Research Assistant
Angela Wong, B.S.  Undergraduate Researcher Aβ42 oligomers in cerebrospinal fluid Nursing Program
Shiela Beroukhim, B.S.  Undergraduate Researcher Effect of GSE fractions on Aβ aggregation Medical Student, UCLA
Tien-Phat Huynh, B.S.  Undergraduate Researcher Stability of individual Aβ oligomers MD/PhD Student, Washington University School of Medicine
Ghiam Yamin, MD, PhD Graduate Student Aβ42 as a therapeutic target in Alzheimer’s disease Residency in Diagnostic Radiology, UC San Diego
Eric Pang, PhD Graduate Student Mass spectrometry of Aβ. Research Fellow, Division of Drug Safety Research, FDA
Mingfeng Yang, PhD Postdoctoral Scholar Computational analysis of Aβ structure and properties. Software Engineer at RED Interactive Agency
Mei-Sha Chen Visiting Scientist Aβ monomer association   
Mohammed Inathayllah, PhD Postdoctoral Scholar Conformational studies and effect of assemblies on amyloid peptides. Senior Research Associate, Stanford School of Medicine
Kenjiro Ono, PhD Postdoctoral Scholar Isolation and properties of individual Aβ40 oligomers. Grape seed extract as therapeutic agent. Lecturer, Kanazawa University, Japan
Samir Maji, PhD Postdoctoral Scholar Aβ Folding and Assembly by Intrinsic Fluorescence. Assistant Professor Biotechnology, Department of Biosciences and Bioengineering, Indian Institute of Technology, Bombay
Noel Lazo, PhD Postdoctoral Scholar Aβ Folding and Assembly by Limited Proteolysis. Assistant Professor & Carlson Chair in Chemistry, Clark University
Gal Bitan, PhD Postdoctoral Scholar 3D Structure of Aβ Assemblies. Associate Professor at UCLA
Marina Kirkatadze, PhD Postdoctoral Scholar Spectroscopic Studies of Aβ Assembly. Deputy director and Head of Biophysics & Conformation Unit, Biochemistry Platform, Analytical R&D at Sanofi Pasteur 
Youcef Fezoui, PhD Postdoctoral Scholar Thermodynamics of Aβ Folding. Director, Licensing & Business Development, Merck, Serono
Dominic Walsh, PhD Postdoctoral Scholar Aβ Oligomerization. Associate Professor of Neurology, Brigham and Women’s Hospital, Harvard Medical School
Deborah Watson, PhD Postdoctoral Scholar APP Processing in Familial AD. Research Assistant Professor; University of Pennsylvania
Erica Fradinger, PhD Postdoctoral Scholar Biological Activity of Soluble Aβ. Assistant Professor of Biology – Whittier College


David B. Teplow, Ph.D.

UCLA Alzheimer’s Disease Research Center
Brain Research Institute
David Geffen School of Medicine
UCLA Health System Research
UCSF California Alzheimer’s Disease Centers

David B. Teplow received B.A. degrees in Biochemistry (1974) and in Bacteriology and Immunology (1975) at the University of California at Berkeley. He did graduate work in Tumor and Molecular Immunology at the University of Washington, where he received his M.S. (1977) and Ph.D. (1981) degrees. His graduate work, which involved protein chemical studies of cell surface receptors, led him to Caltech in Pasadena, where he worked first as a postdoctoral fellow and then as a junior faculty member to develop highly sensitive methods for protein primary structure analysis and to apply these new methods to the study of proteins in the nervous system. From 1991 through 2004, Dr. Teplow was a faculty member in the Departments of Neurology at Brigham and Women’s Hospital and Harvard Medical School, where he established a research program to understand the structural biology of the amyloid beta-protein (Abeta) and its contribution to the pathogenesis of Alzheimer’s disease (AD).

Dr. Teplow joined the faculty at UCLA in 2005, where he currently is a Professor in Residence in the Department of Neurology, a member of the Molecular Biology Institute and the Brain Research Institute, the Director of the Biopolymer Laboratory at UCLA, and the Interim Director of Mary S. Easton Center for Alzheimer’s Disease Research at UCLA. Dr. Teplow is a leader in the areas of the structural biology of amyloid proteins and the biophysics of amyloid assembly. The Teplow laboratory seeks to understand and treat neurodegenerative disorders linked to pathologic protein folding. In AD, Abeta; self-associates to form a variety of oligomeric and polymeric structures with potent neurotoxic activities. Abeta; oligomers have been found in vivo in AD patients and may be the proximate neurotoxins in the disease. To understand how the nascent Abeta; monomer folds and assembles into neurotoxic forms, Dr. Teplow has employed an interdisciplinary strategy comprising in vivo, in vitro, in vacuo, and in silico approaches. The long-term goal is to discover the key factors controlling production of neurotoxic assemblies and then to target these factors in strategies for drug development.

Dr. Teplow has published ~147 peer-reviewed articles, including ~104 original articles and ~43 reviews, book chapters, and commentaries. Dr. Teplow was a founding editorial board member of the Journal of Molecular Neuroscience and the American Journal of Neurodegenerative Disease. He is the Associate Editor-in-Chief of the latter journal and also sits on the editorial boards of Amyloid: The Journal of Protein Folding Disorders, Current Chemical Biology, and The Yemeni Journal of Science.


  • Ph.D., Tumor Immunology, U Washington, 1981
  • M.S., Tumor Immunology, U Washington, 1977
  • B.A., Bacteriology and Immunology, UC Berkeley, 1975
  • B.A., Biochemistry, UC Berkeley, 1974

Teplow laboratory research interests:

The Teplow laboratory seeks to understand and treat diseases associated with the aging process. These include Alzheimer’s disease (AD), Parkinson’s disease, Huntington’s disease, and Lou Gehrig’s disease. The laboratory has special expertise in AD, the most common cause of late-life dementia. A key cause of AD is thought to be a protein called the amyloid beta-protein (Aβ). This protein deposits in the brain to form what are called “amyloid plaques.” Our group has worked to understand how these plaques form and to use this knowledge to design drugs to prevent or treat the disease. Our studies have revealed that Abeta shares properties with other proteins linked to human diseases of aging, therefore the work done on AD is likely to advance efforts to understand and treat these disorders.



Publications *  (Selected peer-reviewed publications)

  1. Rentsendorj A, Sheyn J, Fuchs DT, Daley D, Salumbides BC, Schubloom HE, Hart NJ, Li S, Hayden EY, Teplow DB, Black KL, Koronyo Y, Koronyo-Hamaoui M. (2018) A novel role for osteopontin in macrophage-mediated amyloid-β clearance in Alzheimer’s models. Brain Behav Immun. 67:163-180. PMID: 28860067.  PMID: 28860067 .
  2. Hayden EY, Hoi KK, Lopez J, Inayathullah M, Condron MM, Teplow DB. (2017) Identification of key regions and residues controlling Aβ folding and assembly. Scientific Reports, 7(1):12434. PMID: 28974765.  PMID: 28974765.
  3. Banerjee S, Sun Z, Hayden EY, Teplow DB, Lyubchenko YL. (2017) Nanoscale Dynamics of Amyloid β-42 Oligomers As Revealed by High-Speed Atomic Force Microscopy. ACS Nano. PMID: 29165985.  PMID: 29165985.
  4. Kim B, Do TD, Hayden EY, Teplow DB, Bowers MT, Shea JE. (2016) Aggregation of Chameleon Peptides: Implications of α-Helicity in Fibril Formation. J Phys Chem B. 2016 Apr 1. PMID: 27001160
  5. Hayden EY, Conovaloff JL, Mason A, Bitan G, Teplow DB. (2017) Preparation of pure populations of covalently stabilized amyloid β-protein oligomers of specific sizes. Anal Biochem.518:78-85. PMID: 27810329.  PMID: 27810329 .
  6. Roychaudhuri R, Zheng X, Lomakin A, Maiti P, Condron MM, Benedek GB, Bitan G, Bowers MT, Teplow DB. (2015) Role of Species-Specific Primary Structure Differences in Aβ42 Assembly and Neurotoxicity. ACS Chem Neuroscience. doi: 10.1021/acschemneuro.5b00180. PMID: 26421877
  7. Hayden EY, Yamin G, Beroukhim S, Chen B, Kibalchenko M, Jiang L, Ho L, Wang J, Pasinetti GM, Teplow DB. (2015) Inhibiting amyloid β-protein assembly: Size-activity relationships among grape seed-derived polyphenols. J Neurochem. doi: 10.1111/jnc.13270. PMID: 26228682
  8. Yamin G, Huynh TV, Teplow DB. (2015) Design and characterization of chemically stabilized Aβ42 oligomers. Biochemistry. doi: 10.1021/acs.biochem.5b00318 PMID: 26241378
  9. Roychaudhuri R, Lomakin A, Bernstein S, Zheng X, Condron MM, Benedek GB, Bowers MT, and Teplow DB (2014) Gly25-Ser26 amyloid β-protein structural isomorphs produce distinct Aβ42 conformational dynamics and assembly characteristics. J Mol Biol, 426:2422–2441. PMID:24735871
  10. Roychaudhuri R, Yang M, Deshpande A, Cole GM, Frautschy S, Lomakin A, Benedek GB, Teplow DB.(2013) C-Terminal Turn Stability Determines Assembly Differences between Aβ40 and Aβ42. JMB, 425:292–308. PMID: 23154165
  11. Hayden EY and Teplow DB. (2012) Continuous Flow Reactor for the Production of Stable Amyloid Protein Oligomers. Biochemistry, 51(32), 6342-6349. PMID: 22803680
  12. Roychaudhuri R, Yang M, Condron MM, Teplow DB. (2012) Structural dynamics of the amyloid β-protein monomer folding nucleus.Biochemistry. May 15;51(19):3957-9. PMID: 22551351
  13. Inayathullah M and Teplow DB (2011) Structural dynamics of the ΔE22 (Osaka) familial Alzheimer’s disease-linked amyloid β-protein. Amyloid: J. Prot. Fold. Dis., in press. PMID: 21668291
  14. Matsumura S, Shinoda K, Yamada M, Yokojima S, Inoue M, Ohnishi T, Shimada T, Kikuchi K, Masui D, Hashimoto S, Sato M, Ito A, Akioka M, Takagi S, Nakamura Y, Nemoto K, Hasegawa Y, Takamoto H, Inoue H, Nakamura S, Nabeshima Y, Teplow DB, Kinjo M, and Hoshi M (2011) Two distinct amyloid β-protein (Aβ) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology and toxicity analyses. JBC, 286:11555-11562. PMID: 21292768; PMCID: PMC3064209
  15. Ono K, Condron MM, and Teplow DB (2010) Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid β-protein assembly and toxicity. JBC, 285:23186-23197. PMID: 20452980; PMCID: PMC2906312
  16. Wang J, Santa-Maria I, Ho L, Ksiezak-Reding H, Ono K, Teplow DB, Pasinetti GM (2010) Grape-derived polyphenols attenuate tau neuropathology in a mouse model of Alzheimer’s disease. J Alzheimer’s Dis, 22:653-661. PMID: 20858961
  17. Urbanc B, Betnel M, Cruz L, Bitan G, Teplow DB (2010) Elucidation of amyloid β-protein oligomerization mechanisms: Discrete molecular dynamics study. JACS, 132:4266-4280. PMID: 20218566
  18. Ikeda T, Ono K, Elashoff D, Condron MM, Noguchi-Shinohara M, Yoshita M, Teplow DB, and Yamada M (2010) Cerebrospinal fluid of Alzheimer patients promotes amyloid β-protein oligomerization. J Alzheimer’s Dis, 21:81-86. PMID: 20413863
  19. Walsh DM, Thulin E, Minogue AM, Gustavsson N, Pang E, Teplow DB, Linse S (2009) Aβ facile method for expression and purification of the Alzheimer’s disease-associated amyloid β-peptide. FEBS J, 276:1266-1281. PMID: 19175671; PMCID: PMC2702495
  20. Yamin G, Ruchala P, Teplow DB (2009) A peptide hairpin inhibitor of amyloid β-protein oligomerization and fibrillogenesis. Biochem, 48:11329-11331. PMID: 19877710
  21. Noguchi A, Matsumura S, Dezawa M, Tada M, Yanazawa M, Ito A, Akioka M, Kikuchi S, Sato M, Ideno S, Noda M, Fukunari A, Muramatsu S, Itokazu Y, Sato K, Takahashi H, Teplow DB, Nabeshima Y, Kakita A, Imahori K, and Hoshi M (2009) Isolation and characterization of patient-derived, toxic, high-mass amyloid β-protein (Aβ) assembly from Alzheimer disease brains. J Biol Chem, 284:32895-32905. PMID: 19759000; PMCID: PMC2781705
  22. Maji SK, Ogorzalek Loo RR, Spring SM, Vollers SS, Condron MM, Bitan G, Loo JA, and Teplow DB (2009) Amino acid position-specific contributions to amyloid β-protein oligomerization. J Biol Chem, 284:23580-23591. PMID: 19567875; PMCID: PMC2749133
  23. Ono K, Condron MM, Teplow DB (2009) Structure-neurotoxicity relationships of amyloid β-protein oligomers. PNAS, 106:14745-14750. PMID: 19706468; PMCID: PMC2736424
  24. Murray M, Bernstein S, Nyugen V, Condron MM, Teplow D, Bowers M (2009) Amyloid β-protein: Aβ40 inhibits Aβ42 oligomerization. JACS, 131:6316-6317. PMID: 19385598; PMCID: PMC2697393
  25. Bernstein SL, Dupuis NF, Lazo ND, Wyttenbach T, Condron MM, Bitan G, Teplow DB, Shea J-E, Ruotolo BT, Robinson CV & Bowers MT (2009) Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer’s disease. Nature Chem, 1: 326-331. PMID: 20703363; PMCID: PMC2918915
  26. Murray M, Krone MG, Bernstein SL, Baumketner A, Condron, M, Lazo ND, Teplow DB, Wyttenbach T, Shea J-E, Bowers MT (2009) Amyloid β-protein: Experiment and theory on the 21-30 fragment. J Phys Chem B, 113: 6041-6046. PMID: 19341254; PMCID: PMC2693341
  27. Zaghi J, Goldenson B, Inayathullah M, Lossinsky AS, Masoumi A, Avagyan H, Mahanian M, Bernas M, Weinand M, Rosenthal MJ, Espinosa-JeVrey A, De Vellis JS, Teplow DB, Fiala M (2009) Alzheimer disease macrophages shuttle amyloid-β from neurons to vessels, contributing to amyloid angiopathy. Acta Neuropathol, 117:111-124. PMID: 19139910
  28. Ho L, Chen LH, Wang J, Zhao W, Talcott ST, Ono K, Teplow DB, Humala N, Cheng A, Percival SS, Ferruzzi M, Janle E, Weaver C, Dickstein DL, Pasinetti GM (2009) Heterogeneity in red wine polyphenolic contents differentially influences Alzheimer’s disease-type neuropathology and cognitive deterioration. J Alzheimer’s Dis, 16:59-72. PMID: 19158422; PMCID: PMC2857553
  29. Zhao W, Wang J, Ho, L, Ono K, Teplow DB, Pasinetti GM (2009) Identification of antihypertensive drugs which inhibit amyloid-β protein oligomerization. J Alzheimer’s Dis, 16:49-57. PMID: 19158421
  30. Lam AR, Teplow DB, Stanley HE, and Urbanc B (2008) Effects of the Arctic (Glu22->Gly) mutation on amyloid β-protein folding: Discrete molecular dynamics study. JACS, 130:17413-17422. PMID: 19053400
  31. Ono K, Condron MM, Ho L, Wang J, Zhao W, Pasinetti GM, and Teplow DB (2008) Effects of grape seed-derived polyphenols on amyloid β-protein self-assembly and cytotoxicity. J. Biol Chem, 283: 32176-32187. (This paper was selected as a JBC “Paper of the Week,” an honor accorded to papers in the top 1% of all published, based on significance and overall importance.) PMID: 18815129; PMCID: PMC2583320
  32. Yang M and Teplow DB (2008) Amyloid β-protein monomer folding: free energy landscapes reveal alloform specific differences. J Mol Biol, 384: 450-464. PMID: 18835397; PMCID: PMC2673916
  33. Fluhrer R, Fukumori A, Martin L, Grammer G, Haug-Kröperr M, Klier B, Winkler E, Kremmer E, Condron MM, Teplow DB, Steiner H, and Haass C (2008) Intramembrane proteolysis of GxGD-type aspartyl proteases is slowed by a familial Alzheimer disease-like mutation. J Biol Chem, 283: 30121-30128. PMID: 18768471; PMCID: PMC2573083
  34. Wang J, Ho L, Zhao W, Ono K, Rosensweig C, Chen L, Humala N, Teplow DB, Pasinetti GM (2008) Grape-derived polyphenolics prevent Aβ oligomerization and attenuate cognitive deterioration in a mouse model of Alzheimer’s disease. J Neurosci, 28: 6388-6392. PMID: 18562609; PMCID: PMC2806059
  35. Krone MG, Baumketner A, Bernstein SL, Wyttenbach T, Lazo ND, Teplow DB, Bowers MT, Shea J-E (2008) Effects of familial Alzheimer’s disease mutations on the folding nucleation of the amyloid β-protein. J Mol Biol, 381: 221-228. PMID: 18597778; PMCID: PMC2597412
  36. Ren Y, Strobel GA, Graff JC, Jutila M, Park SG, Gosh S, Teplow D, Condron M, Pang E, Hess WM, and Moore E (2008) Colutellin A, an immunosuppressive peptide from Colletotrichum dematium. Microbiology, 154: 1973-1979. PMID: 18599825
  37. Grant MA, Lazo ND, Lomakin A, Condron MM, Arai H, Yamin G, Rigby AC, and Teplow DB (2007) Familial Alzheimer’s disease mutations alter the stability of the amyloid β-protein monomer folding nucleus. PNAS, 104: 16522-16527. PMID: 17940047; PMCID: PMC2034231
  38. Yun S, Urbanc B, Cruz L, Bitan G, Teplow DB, Stanley HE (2007) Role of electrostatic interactions in amyloid β-protein (A β) oligomer formation: a discrete molecular dynamics study. Biophys J, 92:4064-4077. PMID: 17307823; PMCID: PMC1868995
  39. Hori Y, Hashimoto T, Wakutani Y, Urakami K, Nakashima K, Condron MM, Tsubuki S, Saido TC, Teplow DB, and Iwatsubo T. (2007) The Tottori (D7N) and English (H6R) familial Alzheimer’s disease mutations accelerate Aβ fibril formation without increasing protofibril formation. J Biol Chem, 282:4916-4923. PMID: 17170111

Eric Yale Hayden, Ph.D.

    Assistant Project Scientist
  • Ph.D. and M.S., Physiology and Biophysics, Albert Einstein College of Medicine of Yeshiva University, 2009
  • B.A., Biology, New York University, 2004

Dr. Eric Y. Hayden is an Assistant Project Scientist in the Department of Neurology in the David Geffen School of Medicine at the University of California, Los Angeles. He has a long held curiosity in protein folding and misfolding as it relates to neurodegenerative diseases. His research has examined the biophysical and biochemical properties of amyloid forming proteins, and their oligomeric assemblies. Dr. Hayden’s doctoral work focused on studies of the molecular basis of Parkinson’s disease, examining α-synuclein oligomerization, fibrillation and inhibition. In his postdoctoral work he developed a technique to stabilize large quantities of amyloid β-protein (Aβ) oligomers, the protein that has been implicated as a key neurotoxin in Alzheimer’s disease. He also developed a method to isolate individual oligomers in preparation for structure-activity relationship determination. He has also identified important regions of the Aβ sequence through D-amino acid scanning substitutions, and in collaboration with clinicians, is in the process of biomarker development through studies of the ability of cerebrospinal fluid to inhibit oligomerization. In recent work Dr. Hayden is investigating a mixed dementia mouse model to understand the interplay between stroke and Alzheimer’s disease, and has developed methods to dissociate and isolate stroke affected vs. non-affected neuronal populations from mouse cortex for single cell sequencing to pinpoint genes and pathways responsible for responding to neuronal damage.

He has been recognized for his research through awards including pre-doctoral and post-doctoral training grants from the NIH, the Outstanding Young Alumni Award from The Albany Academies, the 2012 Mazz Prize from the UCLA Department of Neurology, a Rapid Grant Award from the UCLA Claude Pepper Older Americans Independence Center and the UCLA Clinical and Translational Science Institute, and the 2013 Young Investigator Award from the California Southland Chapter of the Alzheimer’s Association, and most recently the 2017 Turken Research Award given by the Sam and Ida Turken Charitable Foundation and the Mary S. Easton Center for Alzheimer’s Disease Research at UCLA.

Dr. Hayden received a Bachelor of Arts in Biology from New York University in 2004, and a M.S. and Ph.D. in Physiology and Biophysics from Albert Einstein College of Medicine in 2007 and 2009 respectively. He performed postdoctoral research with David Teplow, Ph.D. in the Department of Neurology at UCLA, and more recently has worked with Jason Hinman, MD, PhD also in the UCLA Department of Neurology.


1. David Li, Eric Y. Hayden, Koustubh Panda, Dennis J. Stuehr, Haiteng Deng, Denis L. Rousseau and Syun-Ru Yeh. Regulation of the Monomer-Dimer Equilibrium in Inducible Nitric Oxide Synthase by NO. Journal of Biological Chemistry, 2006, 281(12):8197-204. PMID: 16421101.
2. Tsuyoshi Egawa, Jorge Durand, Eric Y. Hayden, Denis L. Rousseau and Syun-Ru Yeh. Design and Evaluation of a Passive Alcove-based Microfluidic Mixer. Analytical Chemistry, 2009, 81 (4), pp 1622–1627. PMID: 19140669
3. Denis L. Rousseau, David Li, Eric Y. Hayden, Haiteng Deng and Syun-Ru Yeh The Smallest Biomolecules: Diatomics and their Interactions with Heme Proteins. Ligand-Protein Interactions in Nitric Oxide Synthase. Book Chapter, Elsevier Science, Amsterdam. Editor: A. Ghosh. 2008, p235-266.
4. Eric Y. Hayden and David B. Teplow. Imperial College Press, London. Editor: Philippe Derreumaux. Alzheimer’s disease: Insights into low molecular weight and cytotoxic aggregates from computer simulations: Molecular basis of amyloid β-protein aggregation and fibril formation. Biophysical characterization of Aβ aggregation. ISBN: 978-1-84816-754-4 and 1-84816-754-7. Pub. Date: Feb 2013.
5. Eric Y. Hayden and David B. Teplow. Continuous Flow Reactor for the Production of Stable Amyloid Protein Oligomers. Biochemistry, 2012, 51(32), 6342-6349. PMID: 22803680
6. Mizwicki MT, Liu G, Fiala M, Magpantay L, Sayre J, Siani A, Mahanian M, Weitzman R, Hayden EY, Rosenthal MJ, Nemere I, Ringman J, Teplow DB. 1α,25-dihydroxyvitamin D3 and resolvin D1 retune the balance between amyloid-β phagocytosis and inflammation in Alzheimer disease patients. Journal of Alzheimer’s Disease, 2012, 34(1).  PMID: 23186989
7. Hayden EY and Teplow DB Amyloid β-protein oligomers and Alzheimer’s disease. Alzheimer’s Research and Therapy, 2013, Nov 29;5(6):60. PMID: 24289820
8. Hayden EY, Yamin G, Beroukhim S, Chen B, Kibalchenko M, Jiang L, Ho L, Wang J, Pasinetti GM, Teplow DB. Inhibiting amyloid β-protein assembly: Size-activity relationships among grape seed-derived polyphenols. J Neurochem. 2015 doi: 10.1111/jnc.13270. PMID: 26228682
9. Hayden EY, Kaur P, Williams TL, Matsui H, Yeh SR, Rousseau DL. Heme Stabilization of α-Synuclein Oligomers during Amyloid Fibril Formation. Biochemistry. 2015 Aug 4;54(30):4599-610. doi: 10.1021/acs.biochem.5b00280. Epub 2015 Jul 24. PMID: 26161848
10. Do TD, Lapointe NE, Nelson R, Krotee P, Hayden EY, Ulrich B, Quan, S, Feinstein SC, Teplow DB, Eisenberg D, Shea J-E, Bowers MT. Amyloid β-Protein C-terminal Fragments: Formation of Cylindrins and β-barrels. J Am Chem Soc. 2015 Dec 23. PMID: 26700445
11. Bilousova T, Miller CA, Poon WW, Vinters HV, Corrada M, Kawas C, Hayden EY, Teplow DB, Glabe C, Albay R, Cole GM, Teng E, Gylys KH. Synaptic Aβ oligomers precede p-tau and differentiate high pathology control cases. American Journal of Pathology, 2016 Jan Vol. 186, Issue 1, 185 – 198. Editor’s Choice article. PMID: 26718979
12. Kim B, Do TD, Hayden EY, Teplow DB, Bowers MT, Shea JE. Aggregation of Chameleon Peptides: Implications of α-Helicity in Fibril Formation. J Phys Chem B. 2016 Apr 1. PMID: 27001160
13. Hayden EY, Conovaloff JL, Mason A, Bitan G, Teplow DB. Preparation of pure populations of covalently stabilized amyloid β-protein oligomers of specific sizes. Anal Biochem. 2017 Feb 1;518:78-85. PMID: 27810329.  PMID: 27810329.
14. Rentsendorj A, Sheyn J, Fuchs DT, Daley D, Salumbides BC, Schubloom HE, Hart NJ, Li S, Hayden EY, Teplow DB, Black KL, Koronyo Y, Koronyo-Hamaoui M. A novel role for osteopontin in macrophage-mediated amyloid-β clearance in Alzheimer’s models. Brain Behav Immun. 2018 Jan;67:163-180. PMID: 28860067 .
15. Hayden EY, Hoi KK, Lopez J, Inayathullah M, Condron MM, Teplow DB. Identification of key regions and residues controlling Aβ folding and assembly. Scientific Reports, 2017, Oct 3;7(1):12434. PMID: 28974765.  PMID: 28974765.
16. Banerjee S, Sun Z, Hayden EY, Teplow DB, Lyubchenko YL. Nanoscale Dynamics of Amyloid β-42 Oligomers As Revealed by High-Speed Atomic Force Microscopy. ACS Nano, 2017, Nov 29. PMID: 29165985.  PMID: 29165985


Mikhail Kibalchenko, Ph.D.

    Postdoctoral Scholar
  • Ph.D. Theory of Condensed Matter, University of Cambridge, UK, 2010
  • M.Sci. Physics, Imperial College London, UK, 2006

Dr. Mikhail Kibalchenko is a postdoctoral fellow who is an expert in quantum mechanics and its implementation in understanding protein structure and dynamics. He has combined quantum mechanics with experimental techniques as a powerful interdisciplinary tool to progress scientific knowledge in the structural studies of infinitely disordered chalcogenide glasses, magnetic environments within carbon nanotubes, techniques for distinguishing hydrogen bonding networks, and most recently transport mechanisms in the ADP/ATP mitochondrial transport proteins. In the Teplow laboratory Dr. Kibalchenko is studying the mechanisms of pathogenesis of Alzheimer’s Disease.

Personal research website:



1. M. Kibalchenko, J. R. Yates, C. Massobrio, A. Pasquarello, Structural composition of first-neighbor shells in GeSe2 and GeSe4 glasses from a first-principles analysis of NMR chemical shifts. The Journal of Physical Chemistry C 115 (15), (2011), pp 7755–7759.

2. M. Kibalchenko, M.C. Payne, J.R. Yates. Magnetic response of single-walled carbon nanotubes in- duced by an external magnetic field. ACS Nano Vol. 5, No. 1 (2011), 537–545.

3. M. Kibalchenko, D. Lee, L. Shao, M. C. Payne, J. J. Titman, J. R. Yates. Distinguishing hydrogen bonding networks in alpha-D-galactose using NMR experiments and first principles calculations. Chemical Physics Letters 498 (2010) 270–276.

4. M. Kibalchenko, J. R. Yates, C. Massobrio, A. Pasquarello. Structural assignments of NMR chemical shifts in GexSe{1-x} glasses through first principles calculations for GeSe2, Ge4Se9, and GeSe crystals. Physical Review B (Rapid Communications) 82 (2010) 020202.

5. M. Kibalchenko, J.R. Yates, A. Pasquarello. First principles investigation of the relation between structural and NMR parameters in vitreous GeO2. Journal of Physics: Condensed Matter 22 (2010) 145501.

6. Hayden EY, Yamin G, Beroukhim S, Chen B, Kibalchenko M, Jiang L, Ho L, Wang J, Pasinetti GM, Teplow DB. (2015) Inhibiting amyloid β-protein assembly: Size-activity relationships among grape seed-derived polyphenols. J Neurochem. doi: 10.1111/jnc.13270. PMID: 26228682

7. E.R.S. Kunji, A. Aleksandrova, M.S. King, H. Majd, V.L. Ashton, E. Cerson, R. Springett, M. Kibalchenko, S. Tavoulari, P.G. Crichton, J.J. Ruprecht, (2016). The transport mechanism of the mitochondrial ADP/ATP carrier. Biochimica et Biophysica Acta Molecular Cell Research. doi:10.1016/j.bbamcr.2016.03.015 PMID: 27001633


Suraj Palaparty

Suraj Palaparty

Undergraduate Researcher

Suraj Palaparty is a third year undergraduate studying Psychobiology.  Suraj discovered an interest in Alzheimer’s research while volunteering with the Youth Movement Against Alzheimer’s and began working in the Teplow Lab in June 2017 under the guidance of Dr. Eric Y. Hayden.  Suraj is studying the kinetics of amyloid β-protein fibril formation.   Suraj most recently worked as an athletic training intern with the UCLA Football team and spends his free time playing intramural sports as a member of the Pi Kappa Phi fraternity.


Ryan Williams

Ryan Williams

Undergraduate Researcher

Ryan Williams is a third year undergraduate majoring in Neuroscience. His interest in developmental biology led him to the lab of Prashanth Rangan at the State University of New York at Albany in the summer of 2017, where he studied RNA helicases and quality control mechanisms in the female germline of Drosophila melanogaster. Since, 2015, he has also conducted research on gambling addiction at the UCLA Gambling Studies Program. Ryan is working with Dr. Eric Hayden in the Teplow lab on characterizing the reaction kinetics of Aβ42 fibril formation mediated by Aβ oligomer nuclei of  different sizes. 

Julia Nakamura


Undergraduate Researcher

Julia Nakamura is a second year undergraduate majoring in Psychobiology. She became interested in Alzheimer’s disease after working with older adults who had various forms of dementia at ONEgeneration Adult Daycare Center. Julia also conducts research in the Mind-Body Laboratory, which tests the effects of childhood adversity on adolescents’ behavior and depression outcomes. Julia works with Dr. Eric Hayden to understand individual oligomer structure and their properties.


Anthony Cannizzaro


Undergraduate Researcher

Anthony Cannizzaro is a third year undergraduate studying Physiological Science. He became interested in Alzheimer’s research when his grandfather developed the disease. Under the guidance of Dr. Eric Y. Hayden, he is researching how cerebrospinal fluid from patients with Alzheimer’s disease affects amyloid β-protein oligomerization. He also works as a supervisor at the Student Activities Center where he assists the manager with preparing for upcoming sporting events. In his free time he enjoys swimming and making music.


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