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Issue 7, 2021
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Does liquid–liquid phase separation drive peptide folding?

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Abstract

Proline–arginine (PR) dipeptide repeats have been shown to undergo liquid–liquid phase separation and are an example of a growing number of intrinsically disordered proteins that can assemble into membraneless organelles. These structures have been posited as nucleation sites for pathogenic protein aggregation. As such, a better understanding of the effects that the increased local concentration and volumetric crowding within droplets have on peptide secondary structure is necessary. Herein we use Fourier transform infrared (FTIR) and two-dimensional infrared (2DIR) spectroscopy to show that formation of droplets by PR20 accompanies changes in the amide-I spectra consistent with folding into poly-proline helical structures.

Graphical abstract: Does liquid–liquid phase separation drive peptide folding?

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Supplementary files

Article information


Submitted
09 Sep 2020
Accepted
28 Dec 2020
First published
29 Dec 2020

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2021,12, 2474-2479
Article type
Edge Article

Does liquid–liquid phase separation drive peptide folding?

D. N. Edun, M. R. Flanagan and A. L. Serrano, Chem. Sci., 2021, 12, 2474
DOI: 10.1039/D0SC04993J

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    [Original citation] - Published by The Royal Society of Chemistry.

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