硫黄素
拉曼光谱
溶菌酶
化学
疏水效应
银纳米粒子
蛋清
动力学
生物物理学
蛋白质二级结构
淀粉样蛋白(真菌学)
纳米颗粒
结晶学
纳米技术
有机化学
生物化学
材料科学
无机化学
医学
物理
疾病
病理
量子力学
生物
光学
阿尔茨海默病
作者
Wei Fan,Xiao Dong Chen,Li Liu,Ning Chen,Xiaoguo Zhou,Zhihong Zhang,Shilin Liu
出处
期刊:Chinese Journal of Chemical Physics
[American Institute of Physics]
日期:2021-08-01
卷期号:34 (4): 393-405
被引量:3
标识
DOI:10.1063/1674-0068/cjcp2104069
摘要
Understanding the influence of nanoparticles on the formation of protein amyloid fibrillation is crucial to extend their application in related biological diagnosis and nanomedicines. In this work, Raman spectroscopy was used to probe the amyloid fibrillation of hen egg-white lysozyme in the presence of silver nanoparticles (Ag-NPs) at different concentrations, combined with atomic force microscopy and thioflavin T (ThT) fluorescence assays. Four representative Raman indicators were utilized to monitor transformation of the protein tertiary and secondary structures at the molecular level: the Trp doublet bands at 1340 and 1360 cm−1, the disulfide stretching vibrational peak at 507 cm−1, the N-Cα-C stretching vibration at 933 cm−1, and the amide I band. All experimental results confirmed the concentration-dependent influence of AgNPs on the hen egg-white lysozyme amyloid fibrillation kinetics. In the presence of AgNPs at low concentration (17 µg/mL), electrostatic interaction of the nanoparticles stabilizes disulfide bonds, and protects the Trp residues from exposure to hydrophilic environment, thus leading to formation of amorphous aggregates rather than fibrils. However, with the action of AgNPs at high concentration (1700 µg/mL), the native disulfide bonds of hen egg-white lysozyme are broken to form Ag-S bonds owing to the competition of electrostatic interaction from a great deal of nanoparticles. As for providing functional surfaces for protein to interact with, AgNPs play a bridge role in direct transformation from α-helices to organized β-sheets. The present investigation sheds light on the controversial effects of AgNPs on the kinetics of hen egg-white lysozyme amyloid fibrillation.
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