Non-covalently embedded oxytocin in alkanethiol monolayer as Zn2+ 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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Bibliographic Details
Published in:Scientific reports 2021-03, Vol.11 (1), p.7051-7051, Article 7051
Main Authors: Attia, Jessica, Nir, Sivan, Mervinetsky, Evgeniy, Balogh, Dora, Gitlin-Domagalska, Agata, Alshanski, Israel, Reches, Meital, Hurevich, Mattan, Yitzchaik, Shlomo
Format: Article
Language:English
Subjects:
631/92/611
639/638/542/970
639/925/350/59
Biosensors
Electrochemistry
Humanities and Social Sciences
Hydrophobicity
Ions
Metal ions
multidisciplinary
Oxytocin
Peptides
Science
Science (multidisciplinary)
Spectroscopy
Zinc
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Summary: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.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-021-85015-w