Slow dissolution kinetics of model peptide fibrils
(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
- Koder Hamid, Mona LU ; Rüter, Axel LU ; Kuczera, Stefan LU and Olsson, Ulf LU
- organization
- publishing date
- 2020-10
- 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
- 2024-09-19 08:47:25
@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}}, }