Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy

David B. Strasfeld, Yun L. Ling, Sang Hee Shim, Martin T. Zanni

Research output: Contribution to journalArticlepeer-review

112 Citations (Scopus)


Amyloid forming proteins have been implicated in many human diseases. The kinetics of amyloid fiber formation are of particular interest because evidence points to intermediate folding structures as potential cytotoxic species. The standard methods for monitoring the kinetics are to use fluorescence or circular dichroism spectroscopy, which do not uniquely resolve secondary structures. In this work, we use a new technology for rapidly scanning 2D-IR spectra that allows us to follow the fiber formation kinetics of the human islet amyloid polypeptide (hIAPP) that is involved in type II diabetes. Spectroscopic markers are identified that uniquely monitor random coil versus β-sheet secondary structures as well as probe β-sheet elongation and stacking. Our measurements provide more rigorous kinetics for the secondary structure evolution of amyloid formation than is available with other techniques.

Original languageEnglish
Pages (from-to)6698-6699
Number of pages2
JournalJournal of the American Chemical Society
Issue number21
Publication statusPublished - 2008 May 28
Externally publishedYes

ASJC Scopus subject areas

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


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