Slow Dissolution Kinetics of Model Peptide Fibrils

Understanding the kinetics of peptide self-assembly is important because of the involvement of peptide amyloid fibrils in several neurodegenerative diseases. In this paper, we have studied the dissolution kinetics of self-assembled model peptide fibrils after a dilution quench. Due to the low concen...

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Bibliographic Details
Published in:International journal of molecular sciences 2020-10, Vol.21 (20), p.7671
Main Authors: Koder Hamid, Mona, Rüter, Axel, Kuczera, Stefan, Olsson, Ulf
Format: Article
Language:English
Subjects:
Aggregates
Amyloid - chemistry
Calorimetry
Chemical Sciences
Dilution
Dissolution
Dissolution kinetics
Experiments
Fibrils
Fysikalisk kemi
Hydrogen Bonding
Hydrogen bonds
Hydrophobic and Hydrophilic Interactions
Kemi
Kinetics
Low concentrations
Natural Sciences
Naturvetenskap
Peptides
Peptides - chemistry
Physical Chemistry
Protein Conformation, beta-Strand
Self-assembly
Titration
β-Amyloid
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Summary:Understanding the kinetics of peptide self-assembly is important because of the involvement of peptide amyloid fibrils in several neurodegenerative diseases. In this paper, we have studied the dissolution kinetics of self-assembled model peptide fibrils after a dilution quench. Due to the low concentrations involved, the experimental method of choice was isothermal titration calorimetry (ITC). We show that the dissolution is a strikingly slow and reaction-limited process, that can be timescale separated from other rapid processes associated with dilution in the ITC experiment. We argue that the rate-limiting step of dissolution involves the breaking up of inter-peptide β-sheet hydrogen bonds, replacing them with peptide-water hydrogen bonds. Complementary pH experiments revealed that the self-assembly involves partial deprotonation of the peptide molecules.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms21207671