Control over the fibrillization yield by varying the oligomeric nucleation propensities of self-assembling peptides.
Commun Chem
; 3(1): 164, 2020 Nov 11.
Article
en En
| MEDLINE
| ID: mdl-36703336
ABSTRACT
Self-assembling peptides are an exemplary class of supramolecular biomaterials of broad biomedical utility. Mechanistic studies on the peptide self-assembly demonstrated the importance of the oligomeric intermediates towards the properties of the supramolecular biomaterials being formed. In this study, we demonstrate how the overall yield of the supramolecular assemblies are moderated through subtle molecular changes in the peptide monomers. This strategy is exemplified with a set of surfactant-like peptides (SLPs) with different ß-sheet propensities and charged residues flanking the aggregation domains. By integrating different techniques, we show that these molecular changes can alter both the nucleation propensity of the oligomeric intermediates and the thermodynamic stability of the fibril structures. We demonstrate that the amount of assembled nanofibers are critically defined by the oligomeric nucleation propensities. Our findings offer guidance on designing self-assembling peptides for different biomedical applications, as well as insights into the role of protein gatekeeper sequences in preventing amyloidosis.
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Colección:
01-internacional
Idioma:
En
Revista:
Commun Chem
Año:
2020
Tipo del documento:
Article
País de afiliación:
Países Bajos