Mechanistic Study on Chiral Nano-Interface Regulation of α-Synuclein Conformational Transition
10.19756/j.issn.0253-3820.251079
- VernacularTitle:手性纳米界面调控α-突触核蛋白构象转变的机制研究
- Author:
Yu-Rong HAN
1
;
Yu-Qi ZHANG
;
Xiu-E JIANG
Author Information
1. 中国科学院长春应用化学研究所,电分析化学国家重点实验室,长春 130022;中国科学技术大学应用化学与工程学院,合肥 230026
- Keywords:
α-Synuclein;
Chiral interface;
Conformational conversion;
Surface-enhanced infrared absorption spectroscopy
- From:
Chinese Journal of Analytical Chemistry
2025;53(5):689-697
- CountryChina
- Language:Chinese
-
Abstract:
The fibrillization of α-synuclein(α-syn)is a key pathological hallmark of Parkinson's disease.Although biointerfaces play a crucial role in α-syn aggregation,the chiral regulation mechanisms remain insufficiently explored.In this work,chiral carbon dots(CD)were employed to construct nanoscale chiral interfaces,and surface-enhanced infrared absorption spectroscopy combined with nanoscale infrared spectroscopy was utilized to investigate the conformational transition ofα-syn at chiral interfaces.The results demonstrated that α-syn primarily adsorbed onto the chiral interfaces via electrostatic interactions,while spatial selectivity further modulated its conformational evolution.Notably,the D-CD interface exhibited high affinity,stabilizingα-syn in its helical conformation,whereas the L-CD and DL-CD interfaces,due to their weaker affinity,exposed aggregation-prone regions,thereby promotingβ-sheet formation and leading to the generation of oligomers and fibrils.This work elucidated the regulatory role of chiral interfaces inα-syn aggregation,providing theoretical insights for the design of protein aggregation inhibitors.
