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A- type EGCG dimer, a new proanthocyanidins dimer from persimmon fruits, interacts with the amino acid residues of Aβ40 which possessed high aggregation-propensity and strongly inhibits its amyloid fibrils formation

Author:
Nie, Rong-zu, Dang, Mei-zhu, Li, Kai-kai, Peng, Jin-ming, Du, Jing, Zhang, Meng-ying, Li, Chun-mei
Source:
Journal of functional foods 2019 v.52 pp. 492-504
ISSN:
1756-4646
Subject:
amino acids, amyloid, binding sites, computer simulation, electrospray ionization mass spectrometry, epigallocatechin gallate, hydrophobic bonding, nuclear magnetic resonance spectroscopy, persimmons, proanthocyanidins
Abstract:
A-type EGCG dimer is a new proanthocyanidins dimer from persimmon fruits. In the present study, we firstly examined the effects of EGCG and A-type EGCG dimer on Aβ40-fibrillization, and then the detailed mechanisms behind the inhibitory effects of polyphenols on Aβ40 amyloid fibrils formation were investigated by PICUP assay, ESI-MS, NMR and molecular docking. Our results confirmed that A-type EGCG dimer exhibited stronger inhibitory effect on the formation of Aβ40 amyloid fibrils. We found that A-type EGCG dimer possessed more binding sites on Aβ40 peptide than EGCG. Notably, compared with EGCG, A-type EGCG dimer could interact with more amino acid residues which possessed obvious aggregation-propensity. And our results also suggested that the hydrophobic interaction was the principal driving force to inhibit the formation of Aβ40 amyloid fibrils by A-type EGCG dimer. We believed that our study could provide useful insights for the design of low-molecular weight inhibitors of Aβ aggregation.
Agid:
6234844