Doliroside A from Dolichos falcata Klein suppressing amyloid β-protein 42 fibrillogenesis: An insight at molecular level

PloS One
Dongpu LiYun Liu

Abstract

A bioactive chemical constituent, doliroside A, from Chinese traditional herbal medicine Dolichos falcata Klein was isolated, purified and identified by 60% ethanol extraction, thin layer chromatography (TLC), high performance liquid chromatography (HPLC) and nuclear magnetic resonance (NMR) spectroscopy. Molecular interaction mechanism between doliroside and amyloid β42 protein was evaluated by thioflavin T fluorescence (ThT), circular dichroism (CD), atomic force microscope (AFM), and differential scanning calorimeter (DSC) from the aspects of kinetics, secondary structure, morphology, and thermodynamics, respectively. Results show that the purity of doliroside A is 99.9% by HPLC, and its chemical structure is identified by 1H- and 13C-NMR. Doliroside A is observed to be concentration-dependent inhibiting the fibrillation of Aβ42 with the IC50 value of 26.57 ± 1.6 μM. CD and DSC results imply that doliroside A can bind to the nuclei and oligomers of Aβ42 to form a stable complex and suppress Aβ42 fibrillation. AFM images show that doliroside A, after bound to the nuclei and oligomers, redirect Aβ42 into off-pathway, amorphous oligomers. These findings not only provide a full insight into the molecular interaction mechanisms b...Continue Reading

References

May 6, 2006·Neurobiology of Aging·Francine GervaisPatrick Tremblay
Nov 4, 2006·Science·Michel Goedert, Maria Grazia Spillantini
Feb 28, 2015·Food Chemistry·Farid KhalloukiRobert W Owen
Jun 30, 2016·ACS Chemical Neuroscience·K RajasekharT Govindaraju

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Methods Mentioned

BETA
NMR
nuclear magnetic resonance
circular dichroism
differential scanning calorimetry
AFM

Software Mentioned

ScanAsyst
Origin Pro
Jasco

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