Design of epidermal growth factor immobilization on 3D biocompatible scaffolds to promote tissue repair and regeneration

Abstract Exogenous application of human epidermal growth factor (hEGF) stimulates epidermal wound healing. The aim of this study was to develop bioconjugates based on hEGF mimicking the protein in its native state and thus suitable for tissue engineering applications, in particular for treating skin...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Teodora Bavaro, Sara Tengattini, Refaya Rezwan, Enrica Chiesa, Caterina Temporini, Rossella Dorati, Gabriella Massolini, Bice Conti, Daniela Ubiali, Marco Terreni
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
Materias:
R
Q
Acceso en línea:https://doaj.org/article/64b432ffe72c459892376f2d7e08c0ad
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:64b432ffe72c459892376f2d7e08c0ad
record_format dspace
spelling oai:doaj.org-article:64b432ffe72c459892376f2d7e08c0ad2021-12-02T14:16:07ZDesign of epidermal growth factor immobilization on 3D biocompatible scaffolds to promote tissue repair and regeneration10.1038/s41598-021-81905-12045-2322https://doaj.org/article/64b432ffe72c459892376f2d7e08c0ad2021-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-81905-1https://doaj.org/toc/2045-2322Abstract Exogenous application of human epidermal growth factor (hEGF) stimulates epidermal wound healing. The aim of this study was to develop bioconjugates based on hEGF mimicking the protein in its native state and thus suitable for tissue engineering applications, in particular for treating skin-related disorders as burns. Ribonuclease A (RNase A) was used to investigate a number of different activated-agarose carriers: cyanogen bromide (CNBr)-activated-agarose and glyoxyl-agarose showed to preserve the appropriate orientation of the protein for receptor binding. EGF was immobilized on these carriers and immobilization yield was evaluated (100% and 12%, respectively). A peptide mapping of unbound protein regions was carried out by LC–MS to take evidence of the residues involved in the immobilization and, consequently, the flexibility and surface accessibility of immobilized EGF. To assess cell proliferative activities, 10, 25, 50, and 100 ng/mL of each immobilized EGF sample were seeded on fibroblast cells and incubated for 24, 48 and 72 h. The immobilized growth factor showed significantly high cell proliferative activity at 50 and 100 ng/mL compared to control and soluble EGF. Although both of the immobilized samples show dose-dependency when seeded with high number of fibroblast cells, CNBr-agarose-EGF showed a significantly high activity at 100 ng/mL and 72 h incubation, compared to glyoxyl-agarose-EGF.Teodora BavaroSara TengattiniRefaya RezwanEnrica ChiesaCaterina TemporiniRossella DoratiGabriella MassoliniBice ContiDaniela UbialiMarco TerreniNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Teodora Bavaro
Sara Tengattini
Refaya Rezwan
Enrica Chiesa
Caterina Temporini
Rossella Dorati
Gabriella Massolini
Bice Conti
Daniela Ubiali
Marco Terreni
Design of epidermal growth factor immobilization on 3D biocompatible scaffolds to promote tissue repair and regeneration
description Abstract Exogenous application of human epidermal growth factor (hEGF) stimulates epidermal wound healing. The aim of this study was to develop bioconjugates based on hEGF mimicking the protein in its native state and thus suitable for tissue engineering applications, in particular for treating skin-related disorders as burns. Ribonuclease A (RNase A) was used to investigate a number of different activated-agarose carriers: cyanogen bromide (CNBr)-activated-agarose and glyoxyl-agarose showed to preserve the appropriate orientation of the protein for receptor binding. EGF was immobilized on these carriers and immobilization yield was evaluated (100% and 12%, respectively). A peptide mapping of unbound protein regions was carried out by LC–MS to take evidence of the residues involved in the immobilization and, consequently, the flexibility and surface accessibility of immobilized EGF. To assess cell proliferative activities, 10, 25, 50, and 100 ng/mL of each immobilized EGF sample were seeded on fibroblast cells and incubated for 24, 48 and 72 h. The immobilized growth factor showed significantly high cell proliferative activity at 50 and 100 ng/mL compared to control and soluble EGF. Although both of the immobilized samples show dose-dependency when seeded with high number of fibroblast cells, CNBr-agarose-EGF showed a significantly high activity at 100 ng/mL and 72 h incubation, compared to glyoxyl-agarose-EGF.
format article
author Teodora Bavaro
Sara Tengattini
Refaya Rezwan
Enrica Chiesa
Caterina Temporini
Rossella Dorati
Gabriella Massolini
Bice Conti
Daniela Ubiali
Marco Terreni
author_facet Teodora Bavaro
Sara Tengattini
Refaya Rezwan
Enrica Chiesa
Caterina Temporini
Rossella Dorati
Gabriella Massolini
Bice Conti
Daniela Ubiali
Marco Terreni
author_sort Teodora Bavaro
title Design of epidermal growth factor immobilization on 3D biocompatible scaffolds to promote tissue repair and regeneration
title_short Design of epidermal growth factor immobilization on 3D biocompatible scaffolds to promote tissue repair and regeneration
title_full Design of epidermal growth factor immobilization on 3D biocompatible scaffolds to promote tissue repair and regeneration
title_fullStr Design of epidermal growth factor immobilization on 3D biocompatible scaffolds to promote tissue repair and regeneration
title_full_unstemmed Design of epidermal growth factor immobilization on 3D biocompatible scaffolds to promote tissue repair and regeneration
title_sort design of epidermal growth factor immobilization on 3d biocompatible scaffolds to promote tissue repair and regeneration
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/64b432ffe72c459892376f2d7e08c0ad
work_keys_str_mv AT teodorabavaro designofepidermalgrowthfactorimmobilizationon3dbiocompatiblescaffoldstopromotetissuerepairandregeneration
AT saratengattini designofepidermalgrowthfactorimmobilizationon3dbiocompatiblescaffoldstopromotetissuerepairandregeneration
AT refayarezwan designofepidermalgrowthfactorimmobilizationon3dbiocompatiblescaffoldstopromotetissuerepairandregeneration
AT enricachiesa designofepidermalgrowthfactorimmobilizationon3dbiocompatiblescaffoldstopromotetissuerepairandregeneration
AT caterinatemporini designofepidermalgrowthfactorimmobilizationon3dbiocompatiblescaffoldstopromotetissuerepairandregeneration
AT rosselladorati designofepidermalgrowthfactorimmobilizationon3dbiocompatiblescaffoldstopromotetissuerepairandregeneration
AT gabriellamassolini designofepidermalgrowthfactorimmobilizationon3dbiocompatiblescaffoldstopromotetissuerepairandregeneration
AT biceconti designofepidermalgrowthfactorimmobilizationon3dbiocompatiblescaffoldstopromotetissuerepairandregeneration
AT danielaubiali designofepidermalgrowthfactorimmobilizationon3dbiocompatiblescaffoldstopromotetissuerepairandregeneration
AT marcoterreni designofepidermalgrowthfactorimmobilizationon3dbiocompatiblescaffoldstopromotetissuerepairandregeneration
_version_ 1718391731688308736