Biophysics / Internet Invited Lecture
DEEP UV RESONANCE RAMAN SPECTROSCOPIC STUDY OF INSULIN FIBRILLATION
Igor K. Lednev, Ludmila A. Popova, Vladimir V. Ermolenkov
Albany, NY, USA
ABSTRACT
Insulin is a protein hormone which controls blood glucose levels. This globular protein undergoes significant structural changes during fibril formation. Such drastic reorganization from mainly alpha-helical to beta-sheet secondary structure of the molecule allowed us to use insulin as a model for studying the protein fibrillation mechanism.
The protein fibrillation process result in formation of highly aggregated gelatinous phase or insoluble particles. This fact limits the application of conventional spectroscopic methods for protein structural characterization.
Deep UV Resonance Raman spectroscopy with excitation below 200 nm was applied to investigate insulin structural reorganizations at all stages of the fibrillation process. In particular, secondary and tertiary structural transformations were probed using Raman spectroscopic signatures of the amide chromophore and aromatic amino acids, phenylalanine and tyrosine, respectively. Other methods used were CD, FTIR, fluorescence and UV absorption spectroscopy. The mechanism of fibrillation will be discussed.
Representing Author:
Igor K. Lednev, University at Albany, SUNY, (Albany, NY, USA)
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