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


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
Issue number34
StatePublished - 27 Aug 2019

Bibliographical note

Funding Information:
S.Y. is the Binjamin H. Birstein Chair in Chemistry. This research was partly supported by the German Research Foundation (DFG) within the Cluster of Excellence “Center for Advancing Electronics Dresden”. TU Dresden gratefully acknowledges computing time by the Center for Information Services and High Performance Computing (ZIH). The authors thank Dr. Vitaly Gutkin for XPS analysis, and Shahar Dery and Dr. Elad Gross for FTIR analysis.

Funding Information:
This investigation was carried out with financial support of the H2020-FETOPEN project Reservoir Computing with Real-time Data for future IT (RECORD-IT) under grant no. 664786. I.L., P.L., and Ž.C. were also supported by the European Union through the European Regional Development Fund—the Competitiveness and Cohesion Operational Programme (KK. and the H2020 CSA Twinning project No. 692194, RBI-T-WINNING.

Publisher Copyright:
© 2019 American Chemical Society.


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