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Structural Organization of Insulin Fibrils Based on Polarized Raman Spectroscopy: Evaluation of Existing Models. | LitMetric

Structural Organization of Insulin Fibrils Based on Polarized Raman Spectroscopy: Evaluation of Existing Models.

J Am Chem Soc

Department of Chemistry, University at Albany, SUNY , 1400 Washington Avenue, Albany, New York 12222, United States.

Published: September 2015

AI Article Synopsis

  • Misfolded proteins can form amyloid fibrils, leading to various neurodegenerative diseases, and traditional structural biology methods struggle to analyze these fibrils effectively.
  • Polarized Raman spectroscopy has been used to gain detailed structural insights into insulin amyloid fibrils, revealing the orientation of key chemical groups, including highly organized β-sheets and disordered α-helices.
  • The study's findings align with and enhance existing models of insulin fibrils, showing that polarized Raman spectroscopy is a valuable tool for understanding the structure of biologically important amyloid fibrils.

Article Abstract

Many different proteins undergo misfolding and self-assemble into amyloid fibrils, resulting in a range of neurodegenerative diseases. The limitations of conventional methods of structural biology for fibril characterization have led to the use of polarized Raman spectroscopy for obtaining quantitative structural information regarding the organization of amyloid fibrils. Herein, we report the orientation of selected chemical groups and secondary structure elements in aligned insulin fibrils, including β-sheets, which possess a high level of orientation in the cross-β core, and α-helices in the disordered portions of the fibrils. Strong orientation of disulfide bonds in amyloid fibrils was also revealed, indicating their association with the fibril core. The determined orientation of chemical groups provides strong constraints for modeling the overall structure of amyloid fibrils, including the core and disordered parts. The developed methodology allows for the validation of structural models proposed in the literature for amyloid fibrils. Specifically, the polarized Raman data obtained herein strongly agreed with two insulin fibril models (Jiménez et al., Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 9196-9201 and Ivanova et al., Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 18990-18995) yet revealed significant qualitative and quantitative differences. This work demonstrates the great potential of polarized Raman spectroscopy for structural characterization of anisotropic biological species.

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Source
http://dx.doi.org/10.1021/jacs.5b07535DOI Listing

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