Core Structure of Amyloid Fibril Proposed from IR-Microscope Linear Dichroism

Hirotsugu Hiramatsu, Yuji Goto, Hironobu Naiki, Teizo Kitagawa

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44 Citations (Scopus)


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 β2-microglobulin and its #21?31 peptide. Furthermore, this approach has shown that the #21?31 peptide consists of two C=O bonds in the β-sheet that makes 0° with the fibril axis, three C=O bonds in the β-sheet inclined by 27° with respect to the fibril axis, four residues in the random coil by 47°, and two residues in possible β-bulge structure by 32°. Plausible structures of the amyloid core in the fibril are proposed by taking account of these results.

Original languageEnglish
Pages (from-to)3008-3009
Number of pages2
JournalJournal of the American Chemical Society
Issue number10
Publication statusPublished - 2004 Mar 17

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry


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