Diarylheptanoids from Rhizomes of Alpinia officinarum Inhibit Aggregation of α-Synuclein

  • J Agric Food Chem. 2017 Aug 9;65(31):6608-6614. doi: 10.1021/acs.jafc.7b02021.
Guangmiao Fu ,  Wei Zhang ,  Dongsheng Du ,  Yu Pong Ng ,  Fanny C F Ip  1 ,  Rongbiao Tong ,  Nancy Y Ip  1
Affiliations
  • 1. Guangdong Provincial Key Laboratory of Brain Science, Disease and Drug Development, HKUST Shenzhen Research Institute , Shenzhen, Guangdong 518057, People's Republic of China.
PMID: 28707886 DOI: 10.1021/acs.jafc.7b02021
Abstract

Two new diarylheptanoids, alpinin A (1) and alpinin B (2), together with 18 known diarylheptanoids (3-20), were isolated from the rhizomes of Alpinia officinarum. Their structures were elucidated by comprehensive spectroscopic analysis, including high-resolution mass spectrometry, infrared spectroscopy, and one- and two-dimensional nuclear magnetic resonance spectroscopy. Structurally, alpinin A is a new member of the small family of oxa-bridged diarylheptanoids and contains the characteristic 2,6-cis-configured tetrahydropyran motif (C1-C5 oxa bridge). The absolute configuration of alpinin A was confirmed by asymmetric total synthesis of the enantiomer (ent-1), corroborating the assignment of the molecular structure. The absolute configuration of alpinin B was determined on the basis of the analysis of the circular dichroism exciton chirality spectrum. We evaluated the inhibitory activity of all isolated diarylheptanoids against α-synuclein Aggregation at 10 μM. Alpinins A and B significantly inhibited α-synuclein Aggregation by 66 and 67%, respectively.

Keywords
Alpinia officinarum; alpinin A; alpinin B; diarylheptanoids; inhibit α-synuclein aggregation.
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