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Updated: Jul 17, 2026

Microfluidic Dry-spinning and Characterization of Regenerated Silk Fibroin Fibers
Published on: September 4, 2017
Core structure of amyloid fibril proposed from IR-microscope linear dichroism
Hirotsugu Hiramatsu1, Yuji Goto, Hironobu Naiki
1Center for Integrative Bioscience, Okazaki National Research Institutes, Myodaiji, Okazaki 444-8585, Japan.
Abstract:
A new approach for studying a peptide conformation of amyloid fibril has been developed. It is based on infrared linear dichroism analysis using an IR-microscope for aligned amyloid fibril. The polarization directions of amide I and II bands were perpendicular similarly for beta2-microglobulin and its #21-31 peptide. Furthermore, this approach has shown that the #21-31 peptide consists of two C=O bonds in the beta-sheet that makes 0 degrees with the fibril axis, three C=O bonds in the beta-sheet inclined by 27 degrees with respect to the fibril axis, four residues in the random coil by 47 degrees , and two residues in possible beta-bulge structure by 32 degrees . Plausible structures of the amyloid core in the fibril are proposed by taking account of these results.
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