Non-covalently embedded oxytocin in alkanethiol monolayer as Zn2+ selective biosensor

Citation:

J. Attia, S. Nir, E. Mervinetsky, D. Balogh, A. Gitlin-Domagalska, I. Alshanski, M. Reches, M. Hurevich, and S. Yitzchaik. 2021. “Non-covalently embedded oxytocin in alkanethiol monolayer as Zn2+ selective biosensor.” Scientific Reports, 11, 1.
Non-covalently embedded oxytocin in alkanethiol monolayer as Zn2+ selective biosensor

Abstract:

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 Zn2+ 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.

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Last updated on 09/17/2021