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

Library Number:
JOUR134965407
Author(s):
Guangmiao Fu, et al.
Source:
Journal of Agricultural and Food Chemistry
Content Type:
Journal Citations
Year:
2017   Volume:   65 (31)   Page(s):   6608-6614
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Two new diarylheptanoids, alpinin A (1) and alpinin B (2), together with 18 known diarylheptanoids (320), 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.

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