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Slow dissolution kinetics of model peptide fibrils

Koder Hamid, Mona LU ; Rüter, Axel LU orcid ; Kuczera, Stefan LU and Olsson, Ulf LU (2020) In International Journal of Molecular Sciences 21(20).
Abstract

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... (More)

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.

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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Dissolution kinetics, Peptides, Self-assembly
in
International Journal of Molecular Sciences
volume
21
issue
20
article number
7671
pages
9 pages
publisher
MDPI AG
external identifiers
  • scopus:85092566481
  • pmid:33081320
ISSN
1661-6596
DOI
10.3390/ijms21207671
language
English
LU publication?
yes
id
53d7479e-38e7-4875-af65-a36e36098742
date added to LUP
2020-11-03 12:49:37
date last changed
2024-05-01 19:39:12
@article{53d7479e-38e7-4875-af65-a36e36098742,
  abstract     = {{<p>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 <i>β</i>–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.</p>}},
  author       = {{Koder Hamid, Mona and Rüter, Axel and Kuczera, Stefan and Olsson, Ulf}},
  issn         = {{1661-6596}},
  keywords     = {{Dissolution kinetics; Peptides; Self-assembly}},
  language     = {{eng}},
  number       = {{20}},
  publisher    = {{MDPI AG}},
  series       = {{International Journal of Molecular Sciences}},
  title        = {{Slow dissolution kinetics of model peptide fibrils}},
  url          = {{http://dx.doi.org/10.3390/ijms21207671}},
  doi          = {{10.3390/ijms21207671}},
  volume       = {{21}},
  year         = {{2020}},
}