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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
KeAi Publishing
2017
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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. |
format | Online Article Text |
id | pubmed-5935176 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | KeAi Publishing |
record_format | MEDLINE/PubMed |
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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