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

Autor: Rong-zu Nie, Mei-zhu Dang, Kai-kai Li, Jin-ming Peng, Jing Du, Meng-ying Zhang, Chun-mei Li
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Zdroj: Journal of Functional Foods, Vol 52, Iss , Pp 492-504 (2019)
Druh dokumentu: article
ISSN: 1756-4646
DOI: 10.1016/j.jff.2018.11.018
Popis: 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.
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