Novel Biospectroscopy for Amyloid Diseases
Monday, March 3, 2008
1:30 p.m., Room 244

Organizer:

Igor K Lednev, University at Albany, SUNY

Speakers:

1:35     Polymorphism in Amyloid Fibrils and Their Assembly Intermediates:  A Moving Target for Structural Analysis  RONALD WETZEL, University of Pittsburgh

2:10      Flow-Induced Alignment of Amyloid Fibrils Revealed by Linear Dichroism  YUJI GOTO, Osaka University

2:45      Structure Determination of Amyloid Peptides and Proteins   ROBERT G GRIFFIN, Massachusetts Institute of Technology (MIT)

3:20      Solution-State Protein Fibril Development Monitored by Large VCD Intensities  LAURENCE A NAFIE, Syracuse University, Shengli Ma, Teresa B Freedman, Rina K Dukor

3:55      Hydrogen-Deuterium Exchange Deep UV Resonance Raman Spectroscopy for Characterizing the Cross-β Core Structure of Amyloid Fibrils  IGOR K LEDNEV, University at Albany, SUNY, Victor Shashilov, Ming Xu

Overview:

Amyloid depositions consisting of fibrils with a cross-b structure have been found in many neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, and prion diseases, etc.  Several mechanisms including inflammatory response, excitotoxicity, synaptic dysfunction, mitochondrial dysfunction, etc. have been proposed for the damaging role of amyloid deposits in the neurodegenerative diseases.  Protein structural transformations on the molecular level during in vitro fibril formation are accompanied by substantial changes in macroscopic properties, such as formation of a gelatinous phase and the formation of insoluble particles.  These changes limit the application of conventional methods for characterizing protein conformational transformations.  Several novel spectroscopic approaches have been recently reported for structural characterization of fibrils including those based on solid state nuclear magnetic resonance (NMR), wide-angle X-ray diffraction analysis, fiber diffraction, high resolution atomic force microscopy (AFM), vibrational circular dichroism (VCD), fluorescent microscopy, UV Raman and IR spectroscopy. All these methods provide complementary information about the structure and formation mechanism of amyloid fibrils.  The leading experts in the field will talk about the latest development and application of novel methodologies for fibrillation problem.  The symposium will be of great interest for a broad community of researches in the arias of spectroscopy, bioanalytical chemistry, biochemistry, biomedicine, as well as engineers designing and developing new instrumentation and data analysis methods.