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Nanoscale Surface Topography Modulates hIAPP Aggregation Pathways at Solid-Liquid Interfaces.

Marcel Hanke¹, Yu Yang¹, Yuxin Ji¹

¹Technical and Macromolecular Chemistry, Paderborn University, Warburger Str. 100, 33098 Paderborn, Germany.

International Journal of Molecular Sciences

|June 2, 2021

Summary

This summary is machine-generated.

Nanoscale surface topography influences protein aggregation. Nanopatterned silicon oxide surfaces retard amyloid fibril formation and enhance amorphous aggregates of the human islet amyloid polypeptide (hIAPP).

Keywords:

adsorption amyloid atomic force microscopy pattern formation self-assembly surface topography

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Area of Science:

Biophysics
Materials Science
Biomedical Engineering

Background:

Solid-liquid interfaces significantly impact protein and peptide aggregation, crucial for molecular biology, biomedicine, and nanotechnology.
Surface chemistry's role in protein aggregation is well-studied, but surface topography's influence remains largely unexplored.

Purpose of the Study:

To investigate how nanoscale surface topography affects the aggregation of the human islet amyloid polypeptide (hIAPP).
To compare hIAPP aggregation on flat versus nanopatterned silicon oxide surfaces.

Main Methods:

Fabrication of nanopatterned silicon oxide surfaces using ion beam irradiation, creating ripple patterns (1.5 nm height, 30 nm periodicity).
Quantitative morphological characterization of hIAPP aggregates using time-lapse atomic force microscopy.

Main Results:

Protein aggregation yielded both amorphous aggregates and amyloid fibrils.
Nanopatterned surfaces led to slower fibrillization and increased amorphous aggregate formation compared to flat surfaces.
Structural differences in amorphous aggregates on nanopatterned surfaces reduced their amyloid nucleation propensity.

Conclusions:

Nanoscale surface topography significantly modulates peptide and protein aggregation pathways.
Surface topography offers a new parameter for controlling protein self-assembly and aggregation.