Issue 41, 2021

Selective and stoichiometric incorporation of ATP by self-assembling amyloid fibrils

Abstract

ATP acts as a biological hydrotrope preventing protein aggregation. Here, we report a novel chimeric peptide, ACC1–13K8, with an unusual capacity to bind and incorporate ATP while self-assembling into amyloid fibrils. The amino acid sequence combines a highly amyloidogenic segment of insulin's A-chain (ACC1–13) and octalysine (K8). Fibrillization requires binding 2 ATP molecules per ACC1–13K8 monomer and is not triggered by adenosine di- and monophosphates (ADP, AMP). Infrared and CD spectra and AFM-based morphological analysis reveal tight and orderly entrapment of ATP within superstructural hybrid peptide–ATP fibrils. The incorporation of ATP is an emergent property of ACC1–13K8 not observed for ACC1–13 and K8 segments separately. We demonstrate how new functionalities (e.g. ATP storage) emerge from synergistic coupling of amyloidogenic segments with non-amyloidogenic peptide ligands, and suggest that ATP's role in protein misfolding is more nuanced than previously assumed.

Graphical abstract: Selective and stoichiometric incorporation of ATP by self-assembling amyloid fibrils

Supplementary files

Article information

Article type
Paper
Submitted
08 Sep 2021
Accepted
01 Okt 2021
First published
04 Okt 2021

J. Mater. Chem. B, 2021,9, 8626-8630

Selective and stoichiometric incorporation of ATP by self-assembling amyloid fibrils

R. Dec, W. Puławski and W. Dzwolak, J. Mater. Chem. B, 2021, 9, 8626 DOI: 10.1039/D1TB01976G

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements