Functionalization of amyloid fibrils via the Bri2 BRICHOS domain

Abstract Amyloid fibrils are mechanically robust and partly resistant to proteolytic degradation, making them potential candidates for scaffold materials in cell culture, tissue engineering, drug delivery and other applications. Such applications of amyloids would benefit from the possibility to fun...

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Autores principales:	Henrik Biverstål, Rakesh Kumar, Anna Katharina Schellhaus, Médoune Sarr, Nico P. Dantuma, Axel Abelein, Jan Johansson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b9caf7651d644f00969a609d822c2cf9
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spelling	oai:doaj.org-article:b9caf7651d644f00969a609d822c2cf92021-12-02T15:11:50ZFunctionalization of amyloid fibrils via the Bri2 BRICHOS domain10.1038/s41598-020-78732-12045-2322https://doaj.org/article/b9caf7651d644f00969a609d822c2cf92020-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-78732-1https://doaj.org/toc/2045-2322Abstract Amyloid fibrils are mechanically robust and partly resistant to proteolytic degradation, making them potential candidates for scaffold materials in cell culture, tissue engineering, drug delivery and other applications. Such applications of amyloids would benefit from the possibility to functionalize the fibrils, for example by adding growth factors or cell attachment sites. The BRICHOS domain is found in a family of human proteins that harbor particularly amyloid-prone regions and can reduce aggregation as well as toxicity of several different amyloidogenic peptides. Recombinant human (rh) BRICHOS domains have been shown to bind to the surface of amyloid-β (Aβ) fibrils by immune electron microscopy. Here we produce fusion proteins between mCherry and rh Bri2 BRICHOS and show that they can bind to different amyloid fibrils with retained fluorescence of mCherry in vitro as well as in cultured cells. This suggests a “generic” ability of the BRICHOS domain to bind fibrillar surfaces that can be used to synthesize amyloid decorated with different protein functionalities.Henrik BiverstålRakesh KumarAnna Katharina SchellhausMédoune SarrNico P. DantumaAxel AbeleinJan JohanssonNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 10, Iss 1, Pp 1-9 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Henrik Biverstål Rakesh Kumar Anna Katharina Schellhaus Médoune Sarr Nico P. Dantuma Axel Abelein Jan Johansson Functionalization of amyloid fibrils via the Bri2 BRICHOS domain
description	Abstract Amyloid fibrils are mechanically robust and partly resistant to proteolytic degradation, making them potential candidates for scaffold materials in cell culture, tissue engineering, drug delivery and other applications. Such applications of amyloids would benefit from the possibility to functionalize the fibrils, for example by adding growth factors or cell attachment sites. The BRICHOS domain is found in a family of human proteins that harbor particularly amyloid-prone regions and can reduce aggregation as well as toxicity of several different amyloidogenic peptides. Recombinant human (rh) BRICHOS domains have been shown to bind to the surface of amyloid-β (Aβ) fibrils by immune electron microscopy. Here we produce fusion proteins between mCherry and rh Bri2 BRICHOS and show that they can bind to different amyloid fibrils with retained fluorescence of mCherry in vitro as well as in cultured cells. This suggests a “generic” ability of the BRICHOS domain to bind fibrillar surfaces that can be used to synthesize amyloid decorated with different protein functionalities.
format	article
author	Henrik Biverstål Rakesh Kumar Anna Katharina Schellhaus Médoune Sarr Nico P. Dantuma Axel Abelein Jan Johansson
author_facet	Henrik Biverstål Rakesh Kumar Anna Katharina Schellhaus Médoune Sarr Nico P. Dantuma Axel Abelein Jan Johansson
author_sort	Henrik Biverstål
title	Functionalization of amyloid fibrils via the Bri2 BRICHOS domain
title_short	Functionalization of amyloid fibrils via the Bri2 BRICHOS domain
title_full	Functionalization of amyloid fibrils via the Bri2 BRICHOS domain
title_fullStr	Functionalization of amyloid fibrils via the Bri2 BRICHOS domain
title_full_unstemmed	Functionalization of amyloid fibrils via the Bri2 BRICHOS domain
title_sort	functionalization of amyloid fibrils via the bri2 brichos domain
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/b9caf7651d644f00969a609d822c2cf9
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Functionalization of amyloid fibrils via the Bri2 BRICHOS domain

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