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Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 PLoS+One 2017 ; 12 (10): ä Nephropedia Template TP
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Doliroside A from Dolichos falcata Klein suppressing amyloid ?-protein 42 fibrillogenesis: An insight at molecular level #MMPMID29084238
Li D; Yu H; Lin Q; Liu Y
PLoS One 2017[]; 12 (10): ä PMID29084238show ga
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 ?42 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 A?42 with the IC50 value of 26.57 ± 1.6 ?M. CD and DSC results imply that doliroside A can bind to the nuclei and oligomers of A?42 to form a stable complex and suppress A?42 fibrillation. AFM images show that doliroside A, after bound to the nuclei and oligomers, redirect A?42 into off-pathway, amorphous oligomers. These findings not only provide a full insight into the molecular interaction mechanisms between A?42 and doliroside A, but also facilitate the development of new native anti-AD drug of doliroside A compound.