Direct Assembly and Metal-Ion Binding Properties of Oxytocin Monolayer on Gold Surfaces

Evgeniy Mervinetsky, Israel Alshanski, Jörg Buchwald, Arezoo Dianat, Ivor Lončarić, Predrag Lazić, Željko Crljen*, Rafael Gutierrez, Gianaurelio Cuniberti, Mattan Hurevich, Shlomo Yitzchaik

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Peptides are very common recognition entities that are usually attached to surfaces using multistep processes. These processes require modification of the native peptides and of the substrates. Using functional groups in native peptides for their assembly on surfaces without affecting their biological activity can facilitate the preparation of biosensors. Herein, we present a simple single-step formation of native oxytocin monolayer on gold surface. These surfaces were characterized by atomic force spectroscopy, spectroscopic ellipsometry, and X-ray photoelectron spectroscopy. We took advantage of the native disulfide bridge of the oxytocin for anchoring the peptide to the Au surface, while preserving the metal-ion binding properties. Self-assembled oxytocin monolayer was used by electrochemical impedance spectroscopy for metal-ion sensing leading to subnanomolar sensitivities for zinc or copper ions.

Original languageAmerican English
Pages (from-to)11114-11122
Number of pages9
JournalLangmuir
Volume35
Issue number34
DOIs
StatePublished - 27 Aug 2019

Bibliographical note

Publisher Copyright:
© 2019 American Chemical Society.

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