Revealing the Nanoarchitectonics of Amyloid β‐Aggregation on Two‐Dimensional Biomimetic Membranes by Surface‐Enhanced Infrared Absorption Spectroscopy

Author:

Zhu Manyu12,Zeng Li3,Li Zihao12,Wang Chen12,Wu Lie1,Jiang Xiue12

Affiliation:

1. State Key Laboratory of Electroanalytical Chemistry C hangchun Institute of Applied Chemistry Chinese Academy of Sciences Changchun Jilin 130022 P. R. China

2. School of Applied Chemistry and Engineering University of Science & Technology of China Hefei Anhui 230026 P. R. China

3. State Key Laboratory of Environmental Chemistry and Ecotoxicology Research Center for Eco-Environmental Sciences Chinese Academy of Sciences Beijing 100085 P. R. China

Abstract

AbstractThe in vivo folding of amyloid β (Aβ) is influenced by many factors among which biomembrane interfaces play an important role. Here, using surface‐enhanced infrared absorption (SEIRA) spectroscopy and atomic force microscopy (AFM), the adsorption, structure, and morphology of Aβ42 aggregating on different two‐dimensional interfaces were investigated. Results show that interfaces facilitate the aggregation of Aβ42 and are conducive to the formation of homogeneous aggregates, while the aggregates vary on different interfaces. On hydrophobic interfaces, strong hydrophobic interactions with the C‐terminus of Aβ42 result in the formation of small oligomers with a small proportion of the β‐sheet structure. On hydrophilic interfaces, hydrogen‐bonding interactions and electrostatic interactions promote the formation of large aggregate particles with β‐sheet structure. The hydration repulsion plays an important role in the interaction of Aβ42 with interfaces. These findings help to understand the nature of Aβ42 adsorption and aggregation on the biomembrane interface and the origin of heterogeneity and polymorphism of Aβ42 aggregates.

Funder

National Science Fund for Distinguished Young Scholars

National Natural Science Foundation of China

Publisher

Wiley

Subject

General Chemistry

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