Affiliation:
1. Department of Immunology Binzhou Medical University Yantai 264003 P. R. China
2. State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics National Center for Magnetic Resonance in Wuhan Innovation Academy for Precision Measurement Science and Technology Chinese Academy of Sciences University of Chinese Academy of Sciences Hubei 430071 P. R. China
3. University of Chinese Academy of Sciences Beijing 100049 P. R. China
4. Optics Valley Laboratory Hubei 430074 P. R. China
Abstract
AbstractThe aggregation of amyloidogenic proteins is often related to the occurrence of neurodegenerative diseases, including fused in sarcoma protein (FUS) in frontotemporal lobar degeneration and amyotrophic lateral sclerosis diseases. Recently, the SERF protein family has been reported to have a significant regulatory effect on amyloid formation, but it is still unclear about the detailed mechanisms of SERF acting on different amyloidogenic proteins. Herein, nuclear magnetic resonance (NMR) spectroscopy and fluorescence spectroscopy were used to explore interactions of ScSERF with three amyloidogenic proteins FUS‐LC, FUS‐Core, and α‐Synuclein. NMR chemical shift perturbations reveal them sharing similar interaction sites on the N‐terminal region of ScSERF. However, the amyloid formation of α‐Synuclein protein is accelerated by ScSERF, while ScSERF inhibits fibrosis of FUS‐Core and FUS‐LC proteins. Both the primary nucleation and the total amount of fibrils produced are detained. Our results suggest a diverse role of ScSERF in regulating the fibril growth of amyloidogenic proteins.
Funder
National Natural Science Foundation of China-Shandong Joint Fund for Marine Science Research Centers
Subject
General Chemistry,Catalysis,Organic Chemistry
Cited by
1 articles.
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