Robert H. Fairclough

Robert Fairclough

Position Title
Associate Professor

Unit
Department of Neurology, School of Medicine

1515 Newton Court, Rm. 510C
Bio

Profile Introduction

My lab studies the molecular mechanics of agonist induced channel activation of the nicotinic acetylcholine receptor. We are also mapping the surface domains of the acetylcholine receptor that stimulate the production of pathogenic antibodies in the disease myasthenia gravis with the intent to bind and remove these Abs and to eliminate the memory B cells that possess the blueprint for making them. Robert H. Fairclough, Ph.D. Emeritus Associate Professor, Department of Neurology University of California, Davis Davis, CA 95616 rhfairclough@ucdavis.edu Phone: 530-754-5005

Research Interests

My lab studies the molecular mechanics of agonist induced channel activation of the nicotinic acetylcholine receptor. We are also mapping the surface domains of the acetylcholine receptor that stimulate the production of pathogenic antibodies in the disease myasthenia gravis.  We have produced a 39 amino acid peptide mimic of the Main Immunogenic Region (MIR) of the Torpedo and the human AChR, and attached it upstream from the human IgG1 heavy chain just to the N-terminal of the hinge region.  This assembles into a disulfide bonded dimer and anti-MIR Abs recognize it.  The hope is to use this or an engineered derivative to remove pathogenic Abs from myasthenic patients serum and to eliminate memory B cells that produce anti-MIR pathogenic Abs. 

Grad Group Affiliations

  • Biochemistry, Molecular, Cellular and Developmental Biology
  • Biophysics

Specialties / Focus

  • Signaling and Excitable Membranes

Courses

  • MCB 120L Biochemistry Lab, Fall

Professional Societies

  • Biophysical Society
  • AAAS

Degrees

  • 1967 BA Chemistry Yale University
  • 1977 PhD Chemistry Columbia University

Publications

Trinh, VB; Foster, AJ; Fairclouigh, RH. 2014. Design, synthesis, and characterization of a 39 amino acid peptide mimic of the main immunogenic region of the Torpedo acetylcholine receptor. J.Molimm. 59, 79-90.

Morell, SW; Trinh VB; Gudipati, E; Friend, A; Page, NA; Agius, MA; Richman, DP; Fairclough, RH. 2014.  Structural characterization of the main immunogenic region of the Torpedo acetylcholine receptor. J. Molimm. 58, 116-131.

Lee, T; Chuang, AR; Marek, M; Doniach, S; and Fairclough, RH. 2009. Redistribution of Terbium Ions Across Acetylcholine Receptor-Enriched Membranes Induce by Agonist Desensitization. Biophys. J. 96:2637-47.

Fairclough, RH. 2006. Recalled to life: resurrection of diffusion-enhanced fluorescence energy transfer. Biophys. J. 91(4):1143-4. Epub 2006 Jun 2.

Fairclough, RH; Agius, MA; Gudipati, E; Silvian, L; Hamaoka, B; Beltzner, CC; Lin, MY; Chuang, AR; and Richman, DP. 2003. Agonist-Induced Transitions of the Acetylcholine Receptor. Ann.NY. Acd. Sci. 998:101-113.

Fairclough, RH; Gudipati, E; Lin, MY; Twaddle, GM; Richman, DP; Burkwall, DA; and Josephs, R.. 1998. A role for alpha(187-199) in the conversion of agonist binding energy to the opening of the ACh receptor ion channel. . Ann. NY Acad. Sci.. 841:87-92

Fairclough, RH; Twaddle, GM; Gudipati, E; Lin, MY; and Richman, DP.. 1998. Differential surface accessibility of alpha(187-199) in the Torpedo ACh receptor alpha-subunits.. J. Mol. Bio.. 282:317-330.

Fairclough,RH; Twaddle,GM; Gudipati,E; Stone, RJS; Richman, DP; Burkwall,DA; and Josephs,R.. 1998. Mapping the mAb 383C Epitope to alpha2(187-199) of the Torpedo Acetylcholine Receptor on the Three-dimensional Model.. J Mol Biol. 282:301-315

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