| Literature DB >> 22334382 |
Chenxuan Wang1, Aihua Yang, Xia Li, Denghua Li, Min Zhang, Huiwen Du, Chao Li, Yuanyuan Guo, Xiaobo Mao, Mingdong Dong, Flemming Besenbacher, Yanlian Yang, Chen Wang.
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. This journal is © The Royal Society of Chemistry 2012Entities:
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Year: 2012 PMID: 22334382 DOI: 10.1039/c2nr11508e
Source DB: PubMed Journal: Nanoscale ISSN: 2040-3364 Impact factor: 7.790