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Non-covalently embedded oxytocin in alkanethiol monolayer as Zn(2+) selective biosensor

Peptides are commonly used as biosensors for analytes such as metal ions as they have natural binding preferences. In our previous peptide-based impedimetric metal ion biosensors, a monolayer of the peptide was anchored covalently to the electrode. Binding of metal ions resulted in a conformational...

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Detalles Bibliográficos
Autores principales: Attia, Jessica, Nir, Sivan, Mervinetsky, Evgeniy, Balogh, Dora, Gitlin-Domagalska, Agata, Alshanski, Israel, Reches, Meital, Hurevich, Mattan, Yitzchaik, Shlomo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8007701/
https://www.ncbi.nlm.nih.gov/pubmed/33782419
http://dx.doi.org/10.1038/s41598-021-85015-w
Descripción
Sumario:Peptides are commonly used as biosensors for analytes such as metal ions as they have natural binding preferences. In our previous peptide-based impedimetric metal ion biosensors, a monolayer of the peptide was anchored covalently to the electrode. Binding of metal ions resulted in a conformational change of the oxytocin peptide in the monolayer, which was measured using electrochemical impedance spectroscopy. Here, we demonstrate that sensing can be achieved also when the oxytocin is non-covalently integrated into an alkanethiol host monolayer. We show that ion-binding cause morphological changes to the dense host layer, which translates into enhanced impedimetric signals compared to direct covalent assembly strategies. This biosensor proved selective and sensitive for Zn(2+) ions in the range of nano- to micro-molar concentrations. This strategy offers an approach to utilize peptide flexibility in monitoring their response to the environment while embedded in a hydrophobic monolayer.