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Shim, Sang-Hee
Shim Research Lab
Research Interests
  • Super-resolution Optical Imaging
  • Single-molecule Biophysics
  • Ultrastructural Dynamics
  • Single-cell Systems Biology

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

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Title
Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR Spectroscopy
Author
Strasfeld, David B.Ling, Yun L.Shim, Sang-HeeZanni, Martin T.
Keywords
2-DIMENSIONAL INFRARED-SPECTROSCOPY; SIMULATION; FIBRILS; PEPTIDE
Issue Date
2008-05
Publisher
AMER CHEMICAL SOC
Citation
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, v.130, no.21, pp.6698 - +
Abstract
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.
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DOI
10.1021/ja801483n
ISSN
0002-7863
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BME_Journal Papers
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