Structural characteristics of the beta-sheet-like human and rat islet amyloid polypeptides as determined by scanning tunneling microscopy

Xiaobo Mao, Xiaojing Ma, Lei Liu, Lin Niu, Yanlian Yang, Chen Wang

Research output: Contribution to journalArticle

Abstract

We demonstrate in this work that scanning tunneling microscopy (STM) provides a useful approach to obtaining structural information about human islet amyloid polypeptide (hIAPP) and rat islet amyloid polypeptide (rIAPP) assembly on highly oriented pyrolytic graphite (HOPG) with sub-molecular resolution. The observed hIAPP and rIAPP lamellae consisted of parallel stripes. The STM images of hIAPPs show multiple molecular folding structures, with an average of 11 amino acid residues for the core regions. In addition, the STM images also reveal the assembly characteristics of rIAPP lamellae and may indicate a secondary structural conformation from random coil to beta-sheet-like on the graphite surface.

Original languageEnglish (US)
Pages (from-to)209-215
Number of pages7
JournalJournal of Structural Biology
Volume167
Issue number3
DOIs
StatePublished - Sep 2009
Externally publishedYes

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Scanning Tunnelling Microscopy
Islet Amyloid Polypeptide
Graphite
Molecular Structure
beta-Strand Protein Conformation
Amino Acids

Keywords

  • Human islet amyloid polypeptide (hIAPP)
  • Peptide folding
  • Rat islet amyloid polypeptide (rIAPP)
  • Scanning tunneling microscopy (STM)

ASJC Scopus subject areas

  • Structural Biology

Cite this

Structural characteristics of the beta-sheet-like human and rat islet amyloid polypeptides as determined by scanning tunneling microscopy. / Mao, Xiaobo; Ma, Xiaojing; Liu, Lei; Niu, Lin; Yang, Yanlian; Wang, Chen.

In: Journal of Structural Biology, Vol. 167, No. 3, 09.2009, p. 209-215.

Research output: Contribution to journalArticle

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