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 journalArticle

97 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)6698-6699
Number of pages2
JournalJournal of the American Chemical Society
Volume130
Issue number21
DOIs
Publication statusPublished - 2008 May 28
Externally publishedYes

Fingerprint

Islet Amyloid Polypeptide
Polypeptides
Infrared spectroscopy
Spectrum Analysis
Amyloid
Kinetics
Fibers
Circular dichroism spectroscopy
Amyloidogenic Proteins
Medical problems
Circular Dichroism
Type 2 Diabetes Mellitus
Elongation
Fluorescence
Technology
Proteins
Scanning
Monitoring

ASJC Scopus subject areas

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

Cite this

Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy. / Strasfeld, David B.; Ling, Yun L.; Shim, Sang-Hee; Zanni, Martin T.

In: Journal of the American Chemical Society, Vol. 130, No. 21, 28.05.2008, p. 6698-6699.

Research output: Contribution to journalArticle

Strasfeld, David B. ; Ling, Yun L. ; Shim, Sang-Hee ; Zanni, Martin T. / Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy. In: Journal of the American Chemical Society. 2008 ; Vol. 130, No. 21. pp. 6698-6699.
@article{919b265577694c11ad6aaee04dbb70eb,
title = "Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy",
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.",
author = "Strasfeld, {David B.} and Ling, {Yun L.} and Sang-Hee Shim and Zanni, {Martin T.}",
year = "2008",
month = "5",
day = "28",
doi = "10.1021/ja801483n",
language = "English",
volume = "130",
pages = "6698--6699",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "21",

}

TY - JOUR

T1 - Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy

AU - Strasfeld, David B.

AU - Ling, Yun L.

AU - Shim, Sang-Hee

AU - Zanni, Martin T.

PY - 2008/5/28

Y1 - 2008/5/28

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=44349183090&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=44349183090&partnerID=8YFLogxK

U2 - 10.1021/ja801483n

DO - 10.1021/ja801483n

M3 - Article

C2 - 18459774

AN - SCOPUS:44349183090

VL - 130

SP - 6698

EP - 6699

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 21

ER -