分析化学2025，Vol.53Issue(5)：689-697,9.DOI:10.19756/j.issn.0253-3820.251079
手性纳米界面调控α-突触核蛋白构象转变的机制研究
Mechanistic Study on Chiral Nano-Interface Regulation of α-Synuclein Conformational Transition
摘要
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.关键词
α-突触核蛋白/手性界面/构象转换/表面增强红外吸收光谱Key words
α-Synuclein/Chiral interface/Conformational conversion/Surface-enhanced infrared absorption spectroscopy引用本文复制引用
韩玉蓉,张宇琦,姜秀娥..手性纳米界面调控α-突触核蛋白构象转变的机制研究[J].分析化学,2025,53(5):689-697,9.基金项目
国家重点研发计划项目(No.2022YFE0113000)和国家自然科学基金项目(No.22025406)资助. Supported by the National Key R&D Program of China(No.2022YFE0113000)and the National Natural Science Foundation of China(No.22025406). （No.2022YFE0113000）
