Observation of molecular inhibition and binding structures of amyloid peptides

Aihua Yang; Xia Li; Denghua Li; Min Zhang; Huiwen Du; Chao Li; Yuanyuan Guo; Xiaobo Mao; Mingdong Dong; Flemming Besenbacher; Yanlian Yang; Chen Wang; Chenxuan Wang

doi:10.1039/c2nr11508e

Observation of molecular inhibition and binding structures of amyloid peptides

Aihua Yang, Xia Li, Denghua Li, Min Zhang, Huiwen Du, Chao Li, Yuanyuan Guo, Xiaobo Mao, Mingdong Dong, Flemming Besenbacher, Yanlian Yang, Chen Wang, Chenxuan Wang

Research output: Contribution to journal › Review article › peer-review

31 Scopus citations

Abstract

Unveiling interactions between labeling molecules and amyloid fibrils is essential to develop new detection methods for studying amyloid structures under various conditions. This review endeavours to reflect the progress in studying interactions between molecular inhibitors and amyloid peptides using a series of experimental approaches, such as X-ray diffraction, nuclear magnetic resonance, scanning probe microscopy, and electron microscopy. The revealed binding mechanisms of anti-amyloid drugs and target proteins could benefit the rational design of drugs for prevention or treatment of amyloidal diseases.

Original language	English (US)
Pages (from-to)	1895-1909
Number of pages	15
Journal	Nanoscale
Volume	4
Issue number	6
DOIs	https://doi.org/10.1039/c2nr11508e
State	Published - Mar 21 2012
Externally published	Yes

ASJC Scopus subject areas

Materials Science(all)

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title = "Observation of molecular inhibition and binding structures of amyloid peptides",

abstract = "Unveiling interactions between labeling molecules and amyloid fibrils is essential to develop new detection methods for studying amyloid structures under various conditions. This review endeavours to reflect the progress in studying interactions between molecular inhibitors and amyloid peptides using a series of experimental approaches, such as X-ray diffraction, nuclear magnetic resonance, scanning probe microscopy, and electron microscopy. The revealed binding mechanisms of anti-amyloid drugs and target proteins could benefit the rational design of drugs for prevention or treatment of amyloidal diseases.",

author = "Aihua Yang and Xia Li and Denghua Li and Min Zhang and Huiwen Du and Chao Li and Yuanyuan Guo and Xiaobo Mao and Mingdong Dong and Flemming Besenbacher and Yanlian Yang and Chen Wang and Chenxuan Wang",

year = "2012",

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doi = "10.1039/c2nr11508e",

language = "English (US)",

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TY - JOUR

T1 - Observation of molecular inhibition and binding structures of amyloid peptides

AU - Yang, Aihua

AU - Li, Xia

AU - Li, Denghua

AU - Zhang, Min

AU - Du, Huiwen

AU - Li, Chao

AU - Guo, Yuanyuan

AU - Mao, Xiaobo

AU - Dong, Mingdong

AU - Besenbacher, Flemming

AU - Yang, Yanlian

AU - Wang, Chen

AU - Wang, Chenxuan

PY - 2012/3/21

Y1 - 2012/3/21

N2 - Unveiling interactions between labeling molecules and amyloid fibrils is essential to develop new detection methods for studying amyloid structures under various conditions. This review endeavours to reflect the progress in studying interactions between molecular inhibitors and amyloid peptides using a series of experimental approaches, such as X-ray diffraction, nuclear magnetic resonance, scanning probe microscopy, and electron microscopy. The revealed binding mechanisms of anti-amyloid drugs and target proteins could benefit the rational design of drugs for prevention or treatment of amyloidal diseases.

AB - Unveiling interactions between labeling molecules and amyloid fibrils is essential to develop new detection methods for studying amyloid structures under various conditions. This review endeavours to reflect the progress in studying interactions between molecular inhibitors and amyloid peptides using a series of experimental approaches, such as X-ray diffraction, nuclear magnetic resonance, scanning probe microscopy, and electron microscopy. The revealed binding mechanisms of anti-amyloid drugs and target proteins could benefit the rational design of drugs for prevention or treatment of amyloidal diseases.

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U2 - 10.1039/c2nr11508e

DO - 10.1039/c2nr11508e

M3 - Review article

C2 - 22334382

AN - SCOPUS:84857824125

SN - 2040-3364

VL - 4

SP - 1895

EP - 1909

JO - Nanoscale

JF - Nanoscale

IS - 6

ER -

Observation of molecular inhibition and binding structures of amyloid peptides

Abstract

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