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Published on: March 21, 2025
Aβ aggregation behavior at interfaces with switchable wettability: a bioinspired perspective to understand amyloid
Yijia Guan1, Dongqin Yu2, Hanjun Sun3
1Laboratory of Chemical Biology, Division of Biological Inorganic Chemistry, State Key Laboratory of Rare Earth Resource Utilization, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, P. R. China. xqu@ciac.ac.cn and Henan Key Laboratory of Materials on Deep-Earth Engineering, School of Materials Science and Engineering, Henan Polytechnic University, Henan, Jiaozuo 454003, P. R. China.
Switchable surface wettability impacts amyloid aggregation. A dynamic polypyrrole/taurocholic acid membrane model showed hydrophobic surfaces, not hydrophilic ones, are key for amyloid-beta 40 adsorption and aggregation.
Area of Science:
- Biomaterials Science
- Surface Chemistry
- Neuroscience
Background:
- Amyloid aggregation is implicated in neurodegenerative diseases.
- Controlling surface properties is crucial for understanding and mitigating aggregation.
- Dynamic surface models offer insights into complex biological processes.
Purpose of the Study:
- To investigate the role of switchable surface wettability in amyloid aggregation.
- To utilize a polypyrrole/taurocholic acid (PPy/TCA) dynamic mimic membrane model.
- To determine the influence of hydrophobic versus hydrophilic surfaces on amyloid-beta 40 (Aβ40) behavior.
Main Methods:
- Fabrication of an amphiphilic taurocholic acid (TCA) doped polypyrrole (PPy) film.
- Employing the PPy/TCA film as a dynamic mimic membrane.
- Assessing Aβ40 adsorption and aggregation on surfaces with varying wettability.
Main Results:
- The PPy/TCA film exhibited switchable surface wettability.
- Hydrophobic surfaces significantly promoted Aβ40 adsorption.
- Hydrophobic surfaces, rather than hydrophilic ones, were found to be critical for Aβ40 aggregation.
Conclusions:
- Surface wettability is a critical factor in modulating amyloid aggregation.
- Hydrophobic interactions play a dominant role in Aβ40 adsorption and subsequent aggregation.
- Dynamic surface models provide valuable platforms for studying amyloid-related phenomena.
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