Strategies for Chalcogenide Thin Film Functionalization.
Journal
Langmuir : the ACS journal of surfaces and colloids
ISSN: 1520-5827
Titre abrégé: Langmuir
Pays: United States
ID NLM: 9882736
Informations de publication
Date de publication:
07 07 2020
07 07 2020
Historique:
pubmed:
6
6
2020
medline:
6
6
2020
entrez:
6
6
2020
Statut:
ppublish
Résumé
We report the functionalization of chalcogenide thin films with biotinylated 12-mer peptides SVSVGMKPSPRP and LLADTTHHRPWT exhibiting a high binding affinity toward inorganic surfaces, on the one hand, and with (3-aminopropyl)triethoxysilane (APTES), on the other hand. The specific biotin moieties were used to bind streptavidin proteins and demonstrate the efficacy of the biofunctionalizated chalcogenide thin films to capture biomolecules. Atomic force microscopy provided high-resolution images of the interfaces, and water contact angle measurements gave insight into the interaction mechanisms. Fourier transform infrared spectroscopy in attenuated total reflection mode provided information about the secondary structure of the bound proteins, thanks to the deconvolution of the amide I band (1700-1600 cm
Identifiants
pubmed: 32501009
doi: 10.1021/acs.langmuir.0c01328
doi:
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM