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- Electrochemical and optical investigation of dental pulp stem cell adhesion on modified porous silicon scaffolds doi link

Auteur(s): Soussi Ines, Mazouz Zouhour, Collart Dutilleul Pierre-Yves, Echabaane Mosaab, Martin Fernandez M., Cloitre T., M'Ghaieth Ridha, Cuisinier F.J.G., Cunin Frédérique, Gergely C., Othmane Ali

(Article) Publié: Colloids And Surfaces B: Biointerfaces, vol. 181 p.489-497 (2019)


Ref HAL: hal-02188386_v1
DOI: 10.1016/j.colsurfb.2019.06.003
WoS: 000481565300056
Exporter : BibTex | endNote
Résumé:

Extensive use of porous silicon (PSi) for tissue engineering is due to its convenient properties as it is both non-toxic and bioresorbable. Moreover, PSi surface modification is an important step to enhance cell adhesion and proliferation. In this work, a combination of optical and electrochemical studies is performed to elaborate a suitable PSi multilayer substrate for cell culture. For this study, we modified PSi surface by silanization and antibody grafting (APTES-anti STRO1), the 12-mer specific peptide to silicon p+type coating and the peptide modified with the antibody recognition sequence. Electrochemical characterization of PSi multilayers is performed to investigate its electrical behavior, determine the optimal measuring conditions and reveal the most stable PSi surfaces. Then, the behavior of dental pulp stem cells (DPSC) was investigated on various modified PSi surfaces. An electrochemical method was applied for the first time monitoring the electrical behavior of stem cell adhesion. The cells electrochemical behavior depends on the nature of the surface coating and the peptide-anti STRO1 improved adhesion and cell spreading onto the PSi surface compared to bare surface and the one coated with the peptide. Fluorescent microscopy revealed that all surface modi cation methods enhance cell adhesion compared to the bare PSi surface. An increased cell number is observed on APTES-anti STRO1, peptide and peptide-anti STRO1 coated PSi. The peptide-anti STRO1 provided the best cell proliferation results suggesting the improved accessibility of the recognition fragment of the antibody anti-STRO1.