Issue 7, 2017

Heparin acts as a structural component of β-endorphin amyloid fibrils rather than a simple aggregation promoter

Abstract

The aggregation promoter heparin is commonly used to study the aggregation kinetics and biophysical properties of protein amyloids. However, the underlying mechanism for amyloid promotion by heparin remains poorly understood. In the case of the neuropeptide β-endorphin that can reversibly adopt a functional amyloid form in nature, aggregation in the presence of heparin leads to a loss of function. Applying correlative optical super-resolution microscopy methods, we show that heparin incorporates into emerging β-endorphin fibrils forming an integral component and is essential for amyloid templating. This will have direct implications on β-endorphin's normal physiological function and raises concerns on the biological relevance of heparin-promoted amyloid models.

Graphical abstract: Heparin acts as a structural component of β-endorphin amyloid fibrils rather than a simple aggregation promoter

Supplementary files

Article information

Article type
Communication
Submitted
08 Dec 2016
Accepted
16 Dec 2016
First published
21 Dec 2016
This article is Open Access
Creative Commons BY license

Chem. Commun., 2017,53, 1273-1276

Heparin acts as a structural component of β-endorphin amyloid fibrils rather than a simple aggregation promoter

N. Nespovitaya, P. Mahou, R. F. Laine, G. S. K. Schierle and C. F. Kaminski, Chem. Commun., 2017, 53, 1273 DOI: 10.1039/C6CC09770G

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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