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

doi:10.1016/j.jsb.2009.05.009

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 journal › Article › peer-review

36 Scopus citations

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 language	English (US)
Pages (from-to)	209-215
Number of pages	7
Journal	Journal of Structural Biology
Volume	167
Issue number	3
DOIs	https://doi.org/10.1016/j.jsb.2009.05.009
State	Published - Sep 2009
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

Structural Biology

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10.1016/j.jsb.2009.05.009

Cite this

@article{8c3706cb5990454482d7363de84d23d2,

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

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.",

keywords = "Human islet amyloid polypeptide (hIAPP), Peptide folding, Rat islet amyloid polypeptide (rIAPP), Scanning tunneling microscopy (STM)",

author = "Xiaobo Mao and Xiaojing Ma and Lei Liu and Lin Niu and Yanlian Yang and Chen Wang",

note = "Funding Information: We gratefully thank Prof. Li, Jia Hu, Yeping Yu from Tsinghua University for the hIAPP and rIAPP. This work was supported by the National Basic Research Program of China (2009CB930100). Financial support from CAS Key Laboratory of Nano Bioeffect and Biosafety is also gratefully acknowledged. ",

year = "2009",

month = sep,

doi = "10.1016/j.jsb.2009.05.009",

language = "English (US)",

volume = "167",

pages = "209--215",

journal = "Journal of Structural Biology",

issn = "1047-8477",

publisher = "Academic Press Inc.",

number = "3",

}

TY - JOUR

T1 - Structural characteristics of the beta-sheet-like human and rat islet amyloid polypeptides as determined by scanning tunneling microscopy

AU - Mao, Xiaobo

AU - Ma, Xiaojing

AU - Liu, Lei

AU - Niu, Lin

AU - Yang, Yanlian

AU - Wang, Chen

N1 - Funding Information: We gratefully thank Prof. Li, Jia Hu, Yeping Yu from Tsinghua University for the hIAPP and rIAPP. This work was supported by the National Basic Research Program of China (2009CB930100). Financial support from CAS Key Laboratory of Nano Bioeffect and Biosafety is also gratefully acknowledged.

PY - 2009/9

Y1 - 2009/9

N2 - 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.

AB - 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.

KW - Human islet amyloid polypeptide (hIAPP)

KW - Peptide folding

KW - Rat islet amyloid polypeptide (rIAPP)

KW - Scanning tunneling microscopy (STM)

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U2 - 10.1016/j.jsb.2009.05.009

DO - 10.1016/j.jsb.2009.05.009

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SN - 1047-8477

VL - 167

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EP - 215

JO - Journal of Structural Biology

JF - Journal of Structural Biology

IS - 3

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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