Related Experiment Video
Updated: Sep 10, 2025

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
Published on: May 22, 2018
Bile acids and polyphenols inhibit succinic anhydride-induced protein succinylation and amyloid aggregation:
Yilin Huang1, Xingli Huo1, Huijun Liu1
1Key Laboratory of Drug-Targeting and Drug Delivery System of the Education Ministry and Sichuan Province, Sichuan Engineering Laboratory for Plant-Sourced Drug and Sichuan Research Center for Drug Precision Industrial Technology, West China School of Pharmacy, Sichuan University, Chengdu, 610041, China.
Abstract:
Lysine succinylation is a major post-translational modification affecting diverse proteins, and its excessive occurrence can lead to protein misfolding and aggregation-hallmarks of various proteinopathies, such as amyloid-β and Tau tangle formation in Alzheimer's disease and islet amyloid polypeptide aggregation in type 2 diabetes. Here, we investigated the inhibitory effects of bile acid metabolites (deoxycholic acid, glycocholic acid, and taurocholic acid sodium) and natural polyphenols (anthocyanin and salidroside) on succinylation and succinylation-induced amyloid aggregation. Succinylation levels were evaluated using the ninhydrin assay before and after treatment, and aggregation behavior and structural alterations were characterized by SDS-PAGE, inverted fluorescence microscopy, and intrinsic fluorescence spectroscopy. Additionally, fluorescence quenching and molecular docking were used to explore the underlying mechanisms. All five small molecules significantly reduced succinylation in a concentration-dependent manner (p < 0.05). Among bile acids, taurocholic acid sodium exhibited the strongest suppression of aggregation (40.99 %), followed by glycocholic acid (28.32 %) and deoxycholic acid (27.94 %). Anthocyanin showed greater inhibition (33.81 %) than salidroside (26.54 %) (all p < 0.05). The results suggest that these small molecules inhibit succinylation-induced aggregation potentially by interacting with proteins and altering their conformations, thereby preventing excessive succinylation at lysine residues. This study provides new insight into the interplay between bile acid metabolism and protein homeostasis and highlights the therapeutic potential of natural compounds in preventing protein aggregation-related diseases.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Indirect-Acting Cholinergic Agonists: Mechanism of Action
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex,...
Bile
Bile is released when dietary fats enter...
Hepatic Drug Excretion: Influencing Factors
Phase II Reactions: Sulfation and Conjugation with α-Amino Acids
Phase II Reactions: Acetylation Reactions
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...

