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Phase Separation in Supramolecular Hydrogels Based on Peptide Self-Assembly from Enzyme-Coated Nanoparticles.
Criado-Gonzalez, Miryam; Fores, Jennifer Rodon; Carvalho, Alain; Blanck, Christian; Schmutz, Marc; Kocgozlu, Leyla; Schaaf, Pierre; Jierry, Loïc; Boulmedais, Fouzia.
Afiliação
  • Criado-Gonzalez M; Université de Strasbourg, CNRS, Institut Charles Sadron UPR 22 , 67034 Strasbourg , France.
  • Fores JR; Institut National de la Santé et de la Recherche Médicale, UMR-S 1121, "Biomatériaux et Bioingénierie" , 67087 Strasbourg , France.
  • Carvalho A; Université de Strasbourg, Faculté de Chirurgie Dentaire, Fédération de Médecine Translationnelle de Strasbourg and Fédération des Matériaux et Nanoscience d'Alsace , 67000 Strasbourg , France.
  • Blanck C; Université de Strasbourg, CNRS, Institut Charles Sadron UPR 22 , 67034 Strasbourg , France.
  • Schmutz M; Université de Strasbourg, CNRS, Institut Charles Sadron UPR 22 , 67034 Strasbourg , France.
  • Kocgozlu L; Université de Strasbourg, CNRS, Institut Charles Sadron UPR 22 , 67034 Strasbourg , France.
  • Schaaf P; Université de Strasbourg, CNRS, Institut Charles Sadron UPR 22 , 67034 Strasbourg , France.
  • Jierry L; Institut National de la Santé et de la Recherche Médicale, UMR-S 1121, "Biomatériaux et Bioingénierie" , 67087 Strasbourg , France.
  • Boulmedais F; Université de Strasbourg, Faculté de Chirurgie Dentaire, Fédération de Médecine Translationnelle de Strasbourg and Fédération des Matériaux et Nanoscience d'Alsace , 67000 Strasbourg , France.
Langmuir ; 35(33): 10838-10845, 2019 08 20.
Article em En | MEDLINE | ID: mdl-31334660
Spatial localization of biocatalysts, such as enzymes, has recently proven to be an effective process to direct supramolecular self-assemblies in a spatiotemporal way. In this work, silica nanoparticles (NPs) functionalized covalently by alkaline phosphatase (NPs@AP) induce the localized growth of self-assembled peptide nanofibers from NPs by dephosphorylation of Fmoc-FFpY peptides (Fmoc: fluorenylmethyloxycarbonyl; F: phenylalanine; Y: tyrosine; p: phosphate group). The fibrillary nanoarchitecture around NPs@AP underpins a homogeneous hydrogel, which unexpectedly undergoes a macroscopic shape change over time. This macroscopic change is due to a phase separation leading to a dense phase (in NPs and nanofibers) in the center of the vial and surrounded by a dilute one, which still contains NPs and peptide self-assemblies. We thus hypothesize that the phase separation is not a syneresis process. Such a change is only observed when the enzymes are localized on the NPs. The dense phase contracts with time until reaching a constant volume after several days. For a given phosphorylated peptide concentration, the dense phase contracts faster when the NPs@AP concentration is increased. For a given NPs@AP concentration, it condenses faster when the peptide concentration increases. We hypothesize that the appearance of a dense phase is not only due to attractive interactions between NPs@AP but also to the strong interactions of self-assembled peptide nanofibers with the enzymes, covalently fixed on the NPs.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeos / Dióxido de Silício / Materiais Revestidos Biocompatíveis / Hidrogéis / Fosfatase Alcalina / Nanopartículas Idioma: En Revista: Langmuir Assunto da revista: QUIMICA Ano de publicação: 2019 Tipo de documento: Article País de afiliação: França País de publicação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeos / Dióxido de Silício / Materiais Revestidos Biocompatíveis / Hidrogéis / Fosfatase Alcalina / Nanopartículas Idioma: En Revista: Langmuir Assunto da revista: QUIMICA Ano de publicação: 2019 Tipo de documento: Article País de afiliação: França País de publicação: Estados Unidos