Heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides

Abstract Heparan sulfates (HSs) modulate tissue elasticity in physiopathological conditions by interacting with various matrix constituents as tropoelastin and elastin-derived peptides. HSs bind also to protein moieties accelerating amyloid formation and influencing cytotoxic properties of insoluble...

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Autores principales:	Federica Boraldi, Pasquale Moscarelli, Brigida Bochicchio, Antonietta Pepe, Anna M. Salvi, Daniela Quaglino
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/8c820a60bdf24a928d8f6ac0b53ba66d
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spelling	oai:doaj.org-article:8c820a60bdf24a928d8f6ac0b53ba66d2021-12-02T15:07:47ZHeparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides10.1038/s41598-018-21472-02045-2322https://doaj.org/article/8c820a60bdf24a928d8f6ac0b53ba66d2018-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-21472-0https://doaj.org/toc/2045-2322Abstract Heparan sulfates (HSs) modulate tissue elasticity in physiopathological conditions by interacting with various matrix constituents as tropoelastin and elastin-derived peptides. HSs bind also to protein moieties accelerating amyloid formation and influencing cytotoxic properties of insoluble fibrils. Interestingly, amyloidogenic polypeptides, despite their supposed pathogenic role, have been recently explored as promising bio-nanomaterials due to their unique and interesting properties. Therefore, we investigated the interactions of HSs, obtained from different sources and exhibiting various degree of sulfation, with synthetic amyloidogenic elastin-like peptides (ELPs), also looking at the effects of these interactions on cell viability and cell behavior using in vitro cultured fibroblasts, as a prototype of mesenchymal cells known to modulate the soft connective tissue environment. Results demonstrate, for the first time, that HSs, with differences depending on their sulfation pattern and chain length, interact with ELPs accelerating aggregation kinetics and amyloid-like fibril formation as well as self-association. Furthermore, these fibrils do not negatively affect fibroblasts’ cell growth and parameters of redox balance, and influence cellular adhesion properties. Data provide information for a better understanding of the interactions altering the elastic component in aging and in pathologic conditions and may pave the way for the development of composite matrix-based biomaterials.Federica BoraldiPasquale MoscarelliBrigida BochicchioAntonietta PepeAnna M. SalviDaniela QuaglinoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Federica Boraldi Pasquale Moscarelli Brigida Bochicchio Antonietta Pepe Anna M. Salvi Daniela Quaglino Heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides
description	Abstract Heparan sulfates (HSs) modulate tissue elasticity in physiopathological conditions by interacting with various matrix constituents as tropoelastin and elastin-derived peptides. HSs bind also to protein moieties accelerating amyloid formation and influencing cytotoxic properties of insoluble fibrils. Interestingly, amyloidogenic polypeptides, despite their supposed pathogenic role, have been recently explored as promising bio-nanomaterials due to their unique and interesting properties. Therefore, we investigated the interactions of HSs, obtained from different sources and exhibiting various degree of sulfation, with synthetic amyloidogenic elastin-like peptides (ELPs), also looking at the effects of these interactions on cell viability and cell behavior using in vitro cultured fibroblasts, as a prototype of mesenchymal cells known to modulate the soft connective tissue environment. Results demonstrate, for the first time, that HSs, with differences depending on their sulfation pattern and chain length, interact with ELPs accelerating aggregation kinetics and amyloid-like fibril formation as well as self-association. Furthermore, these fibrils do not negatively affect fibroblasts’ cell growth and parameters of redox balance, and influence cellular adhesion properties. Data provide information for a better understanding of the interactions altering the elastic component in aging and in pathologic conditions and may pave the way for the development of composite matrix-based biomaterials.
format	article
author	Federica Boraldi Pasquale Moscarelli Brigida Bochicchio Antonietta Pepe Anna M. Salvi Daniela Quaglino
author_facet	Federica Boraldi Pasquale Moscarelli Brigida Bochicchio Antonietta Pepe Anna M. Salvi Daniela Quaglino
author_sort	Federica Boraldi
title	Heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides
title_short	Heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides
title_full	Heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides
title_fullStr	Heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides
title_full_unstemmed	Heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides
title_sort	heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/8c820a60bdf24a928d8f6ac0b53ba66d
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Heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides

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