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 hydrogen bonds. Complementary pH experiments revealed that the self-assembly involves partial deprotonation of the peptide molecules.
journal_name
Int J Mol Scijournal_title
International journal of molecular sciencesauthors
Koder Hamid M,Rüter A,Kuczera S,Olsson Udoi
10.3390/ijms21207671subject
Has Abstractpub_date
2020-10-16 00:00:00issue
20issn
1422-0067pii
ijms21207671journal_volume
21pub_type
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