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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
Published on: July 17, 2019
Common motifs in protein self-assembly.
Mark R H Krebs1, Kristin R Domike, Danielle Cannon
1Biological and Soft Systems, Cavendish Laboratory, University of Cambridge, JJ Thomson Avenue, Cambridge, CB3 0HE, UK. mrhk2@cam.ac.uk
Faraday Discussions
|December 4, 2008
Summary
Misfolded proteins form amyloid fibrils implicated in diseases. These fibrils can assemble into higher-order structures, revealing a universal protein self-assembly mechanism with implications for disease aetiology.
Area of Science:
- Biochemistry
- Biophysics
- Materials Science
Background:
- Protein misfolding and amyloid fibril formation are linked to age-related diseases.
- Amyloid fibrils can self-assemble into higher-order structures beyond isolated fibrils.
- These higher-order assemblies resemble spherulites found in synthetic polymers.
Purpose of the Study:
- To investigate the kinetics of amyloid fibril growth in different proteins.
- To explore protein self-assembly around the isoelectric point.
- To understand the role of salt concentration on particle formation and structure.
Main Methods:
- Kinetic analysis of fibril growth.
- Microscopy for structural observation.
- Small-angle X-ray scattering (SAXS).
- Thioflavin T staining.
- Fourier-transform infrared spectroscopy (FTIR).
Main Results:
- Identified similarities and differences in fibril growth kinetics across proteins.
- Demonstrated generic particulate self-assembly of proteins near their isoelectric point.
- Showed that salt concentration significantly affects particle growth.
- Confirmed amyloid-like beta-sheet structures within assembled particles, especially in salt-free conditions.
Conclusions:
- Protein self-assembly into higher-order structures is a universal phenomenon.
- Amyloid-like beta-sheet structures are fundamental to diverse protein self-assembly pathways.
- Understanding these assembly mechanisms is crucial for disease aetiology and therapeutic strategies.
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