Cargando…
Functionalization of amyloid fibrils via the Bri2 BRICHOS domain
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 functionaliz...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7730125/ https://www.ncbi.nlm.nih.gov/pubmed/33303867 http://dx.doi.org/10.1038/s41598-020-78732-1 |
_version_ | 1783621612360171520 |
---|---|
author | Biverstål, Henrik Kumar, Rakesh Schellhaus, Anna Katharina Sarr, Médoune Dantuma, Nico P. Abelein, Axel Johansson, Jan |
author_facet | Biverstål, Henrik Kumar, Rakesh Schellhaus, Anna Katharina Sarr, Médoune Dantuma, Nico P. Abelein, Axel Johansson, Jan |
author_sort | Biverstål, Henrik |
collection | PubMed |
description | 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 | Online Article Text |
id | pubmed-7730125 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-77301252020-12-14 Functionalization of amyloid fibrils via the Bri2 BRICHOS domain Biverstål, Henrik Kumar, Rakesh Schellhaus, Anna Katharina Sarr, Médoune Dantuma, Nico P. Abelein, Axel Johansson, Jan Sci Rep Article 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. Nature Publishing Group UK 2020-12-10 /pmc/articles/PMC7730125/ /pubmed/33303867 http://dx.doi.org/10.1038/s41598-020-78732-1 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Biverstål, Henrik Kumar, Rakesh Schellhaus, Anna Katharina Sarr, Médoune Dantuma, Nico P. Abelein, Axel Johansson, Jan Functionalization of amyloid fibrils via the Bri2 BRICHOS domain |
title | 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_short | Functionalization of amyloid fibrils via the Bri2 BRICHOS domain |
title_sort | functionalization of amyloid fibrils via the bri2 brichos domain |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7730125/ https://www.ncbi.nlm.nih.gov/pubmed/33303867 http://dx.doi.org/10.1038/s41598-020-78732-1 |
work_keys_str_mv | AT biverstalhenrik functionalizationofamyloidfibrilsviathebri2brichosdomain AT kumarrakesh functionalizationofamyloidfibrilsviathebri2brichosdomain AT schellhausannakatharina functionalizationofamyloidfibrilsviathebri2brichosdomain AT sarrmedoune functionalizationofamyloidfibrilsviathebri2brichosdomain AT dantumanicop functionalizationofamyloidfibrilsviathebri2brichosdomain AT abeleinaxel functionalizationofamyloidfibrilsviathebri2brichosdomain AT johanssonjan functionalizationofamyloidfibrilsviathebri2brichosdomain |