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Smart biomaterials: Surfaces functionalized with proteolytically stable osteoblast-adhesive peptides

Engineered scaffolds for bone tissue regeneration are designed to promote cell adhesion, growth, proliferation and differentiation. Recently, covalent and selective functionalization of glass and titanium surfaces with an adhesive peptide (HVP) mapped on [351–359] sequence of human Vitronectin allow...

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Detalles Bibliográficos
Autores principales: Zamuner, Annj, Brun, Paola, Scorzeto, Michele, Sica, Giuseppe, Castagliuolo, Ignazio, Dettin, Monica
Formato: Online Artículo Texto
Lenguaje:English
Publicado: KeAi Publishing 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5935176/
https://www.ncbi.nlm.nih.gov/pubmed/29744421
http://dx.doi.org/10.1016/j.bioactmat.2017.05.004
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author Zamuner, Annj
Brun, Paola
Scorzeto, Michele
Sica, Giuseppe
Castagliuolo, Ignazio
Dettin, Monica
author_facet Zamuner, Annj
Brun, Paola
Scorzeto, Michele
Sica, Giuseppe
Castagliuolo, Ignazio
Dettin, Monica
author_sort Zamuner, Annj
collection PubMed
description Engineered scaffolds for bone tissue regeneration are designed to promote cell adhesion, growth, proliferation and differentiation. Recently, covalent and selective functionalization of glass and titanium surfaces with an adhesive peptide (HVP) mapped on [351–359] sequence of human Vitronectin allowed to selectively increase osteoblast attachment and adhesion strength in in vitro assays, and to promote osseointegration in in vivo studies. For the first time to our knowledge, in this study we investigated the resistance of adhesion sequences to proteolytic digestion: HVP was completely cleaved after 5 h. In order to overcome the enzymatic degradation of the native peptide under physiological conditions we synthetized three analogues of HVP sequence. A retro-inverted peptide D-2HVP, composed of D amino acids, was completely stable in serum-containing medium. In addition, glass surfaces functionalized with D-2HVP increased human osteoblast adhesion as compared to the native peptide and maintained deposition of calcium. Interestingly, D-2HVP increased expression of IBSP, VTN and SPP1 genes as compared to HVP functionalized surfaces. Total internal reflection fluorescence microscope analysis showed cells with numerous filopodia spread on D-2HVP-functionalized surfaces. Therefore, the D-2HVP sequence is proposed as new osteoblast adhesive peptide with increased bioactivity and high proteolytic resistance.
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spelling pubmed-59351762018-05-09 Smart biomaterials: Surfaces functionalized with proteolytically stable osteoblast-adhesive peptides Zamuner, Annj Brun, Paola Scorzeto, Michele Sica, Giuseppe Castagliuolo, Ignazio Dettin, Monica Bioact Mater Article Engineered scaffolds for bone tissue regeneration are designed to promote cell adhesion, growth, proliferation and differentiation. Recently, covalent and selective functionalization of glass and titanium surfaces with an adhesive peptide (HVP) mapped on [351–359] sequence of human Vitronectin allowed to selectively increase osteoblast attachment and adhesion strength in in vitro assays, and to promote osseointegration in in vivo studies. For the first time to our knowledge, in this study we investigated the resistance of adhesion sequences to proteolytic digestion: HVP was completely cleaved after 5 h. In order to overcome the enzymatic degradation of the native peptide under physiological conditions we synthetized three analogues of HVP sequence. A retro-inverted peptide D-2HVP, composed of D amino acids, was completely stable in serum-containing medium. In addition, glass surfaces functionalized with D-2HVP increased human osteoblast adhesion as compared to the native peptide and maintained deposition of calcium. Interestingly, D-2HVP increased expression of IBSP, VTN and SPP1 genes as compared to HVP functionalized surfaces. Total internal reflection fluorescence microscope analysis showed cells with numerous filopodia spread on D-2HVP-functionalized surfaces. Therefore, the D-2HVP sequence is proposed as new osteoblast adhesive peptide with increased bioactivity and high proteolytic resistance. KeAi Publishing 2017-05-18 /pmc/articles/PMC5935176/ /pubmed/29744421 http://dx.doi.org/10.1016/j.bioactmat.2017.05.004 Text en © 2017 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Article
Zamuner, Annj
Brun, Paola
Scorzeto, Michele
Sica, Giuseppe
Castagliuolo, Ignazio
Dettin, Monica
Smart biomaterials: Surfaces functionalized with proteolytically stable osteoblast-adhesive peptides
title Smart biomaterials: Surfaces functionalized with proteolytically stable osteoblast-adhesive peptides
title_full Smart biomaterials: Surfaces functionalized with proteolytically stable osteoblast-adhesive peptides
title_fullStr Smart biomaterials: Surfaces functionalized with proteolytically stable osteoblast-adhesive peptides
title_full_unstemmed Smart biomaterials: Surfaces functionalized with proteolytically stable osteoblast-adhesive peptides
title_short Smart biomaterials: Surfaces functionalized with proteolytically stable osteoblast-adhesive peptides
title_sort smart biomaterials: surfaces functionalized with proteolytically stable osteoblast-adhesive peptides
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5935176/
https://www.ncbi.nlm.nih.gov/pubmed/29744421
http://dx.doi.org/10.1016/j.bioactmat.2017.05.004
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