Issue 6, 2024

Amyloid engineering – how terminal capping modifies morphology and secondary structure of supramolecular peptide aggregates

Abstract

The effects of peptide N- and C-termini on aggregation behavior have been scarcely studied. Herein, we examine (105–115) peptide fragments of transthyretin (TTR) containing various functional groups at both termini and study their impact on the morphology and the secondary structure. We synthesized TTR(105–115) peptides functionalized with α-amino (H-), N-acetyl-α-amino (Ac-) or N,N-dimethyl-α-amino (DiMe-) groups at the N-terminus, and with amide (–NH2) or carboxyl (–OH) functions at the C-terminus. We also investigated quasi-racemic mixtures by mixing the L-enantiomers with the D-enantiomer capped by H- and –NH2 groups. We observed that fibril formation is promoted by the sufficient number of hydrogen bonds at peptides’ termini. Moreover, the final morphology of the aggregates can be controlled by the functional groups at the N-terminus. Remarkably, all quasi-racemic mixtures resulted in the robust formation of fibrils. Overall, this work illustrates how modifications of peptide termini may help to engineer supramolecular aggregates with a predicted morphology.

Graphical abstract: Amyloid engineering – how terminal capping modifies morphology and secondary structure of supramolecular peptide aggregates

Supplementary files

Article information

Article type
Paper
Submitted
10 Oct 2023
Accepted
13 Jan 2024
First published
23 Jan 2024

Biomater. Sci., 2024,12, 1590-1602

Amyloid engineering – how terminal capping modifies morphology and secondary structure of supramolecular peptide aggregates

M. Grelich-Mucha, T. Bachelart, V. Torbeev, K. Ożga, Ł. Berlicki and J. Olesiak-Bańska, Biomater. Sci., 2024, 12, 1590 DOI: 10.1039/D3BM01641B

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