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Related Experiment Video

Updated: Jun 17, 2025

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Published on: July 14, 2010

Surface effects on functional amyloid formation.

Alexander J Dear^1,2, Georg Meisl¹, Christopher G Taylor¹

¹Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.

|August 13, 2024

Summary

This summary is machine-generated.

Surface interactions significantly influence the formation of functional amyloids by Pseudomonas FapC protein. This study reveals that surfaces catalyze amyloid nucleation, impacting biofilm formation and antimicrobial resistance.

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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

Area of Science:

Microbiology
Biochemistry
Materials Science

Background:

Functional amyloids from Pseudomonas FapC protein are crucial for bacterial biofilms.
These biofilms contribute to chronic infections and antimicrobial resistance.

Purpose of the Study:

To investigate the role of surfaces in FapC functional amyloid formation.
To understand the mechanisms of amyloid nucleation and catalysis.

Main Methods:

Kinetic experiments and mechanistic modeling were employed.
The influence of reaction vessel surfaces and microdroplets on nucleation was studied.
Nanoparticles with tailored surface properties were used to tune catalysis.

Main Results:

Amyloid fibril nucleation is predominantly heterogeneous, catalyzed by reaction vessel walls.
Removing interfaces slows primary nucleation, revealing a secondary nucleation step catalyzed by existing fibrils.
Nucleation rate is controlled by FapC binding strength to catalytic sites and surface area, not charge or hydrophilicity.

Conclusions:

Surface chemistry and area are critical factors in controlling FapC amyloid nucleation.
Protein aggregation and fibril nucleation are fundamentally heterogeneous processes.
Experimental design, including reaction vessel surface properties, is crucial for studying amyloid formation.