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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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Surfactant effects on amyloid aggregation kinetics.

Ran Friedman¹, Amedeo Caflisch

¹Department of Biochemistry, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland. ran.friedman@lnu.se

Journal of Molecular Biology

|October 25, 2011

Summary

This summary is machine-generated.

Surfactants significantly impact amyloid fibril formation kinetics, especially for peptides with low aggregation propensity. Mixed oligomers and transient fibrillar defects explain observed kinetic behaviors.

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Area of Science:

Biophysics
Computational Chemistry
Materials Science

Background:

Surfactants, such as fatty acids, are known to influence amyloid fibril formation kinetics.
The precise structures of mixed peptide-surfactant assemblies and their interactions remain poorly understood.

Purpose of the Study:

To investigate the aggregation kinetics of amyloidogenic peptides in the presence of amphiphilic lipids using coarse-grained simulations.
To elucidate the role of surfactants in modulating peptide self-assembly pathways and fibril formation.

Main Methods:

Coarse-grained molecular dynamics simulations were employed to model peptide-surfactant systems.
Analysis focused on aggregation kinetics, including lag phase duration and the formation of mixed oligomers.

Main Results:

Surfactant influence on peptide self-assembly kinetics is inversely proportional to the peptide's intrinsic fibril formation propensity.
Weakly aggregating peptides exhibit an increased lag phase due to mixed oligomer formation, driven by hydrophobic interactions and entropy.
A transient peak in surfactant attachment to growing fibrils was observed, linked to temporary fibrillar defects with exposed hydrophobic patches.

Conclusions:

Surfactants play a crucial role in modulating amyloid formation, particularly for less aggregation-prone peptides.
The formation of mixed oligomers and transient fibrillar defects provides a mechanistic explanation for observed kinetic phenomena, including fluorescence variations.
Findings offer insights into the complex interplay between peptides and lipids during amyloid self-assembly.