期刊
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY
卷 192, 期 -, 页码 -出版社
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.ejmech.2020.112197
关键词
Protein misfolding disease; Amyloidogenic protein; Protein aggregation; Inhibitor; Non-polyphenolic natural products
资金
- Natural Science Foundation of China (NSFC) [31671195, 81901302, 31971066]
- Front Youth Academic Team Program of HUST
- Integrated Innovative Team for Major Human Diseases Program of Tongji Medical College, HUST
Protein misfolding diseases (PMDs) are chronic and progressive, with no effective therapy so far. Aggregation and misfolding of amyloidogenic proteins are closely associated with the onset and progression of PMDs, such as amyloid-beta (A beta) in Alzheimer's disease, alpha-Synuclein (alpha-Syn) in Parkinson's disease and human islet amyloid polypeptide (hIAPP) in type 2 diabetes. Inhibiting toxic aggregation of amyloidogenic proteins is regarded as a promising therapeutic approach in PMDs. The past decade has witnessed the rapid progresses of this field, dozens of inhibitors have been screened and verified in vitro and in vivo, demonstrating inhibitory effects against the aggregation and misfolding of amyloidogenic proteins, together with beneficial effects. Natural products are major sources of small molecule amyloid inhibitors, a number of natural derived compounds have been identified with great bioactivities and translational prospects. Here, we review the non-polyphenolic natural inhibitors that potentially applicable for PMDs treatment, along with their working mechanisms. Future directions are proposed for the development and clinical applications of these inhibitors. (c) 2020 Elsevier Masson SAS. All rights reserved.
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