Electronic structure of dipeptides in the gas-phase and as an adsorbed monolayer

Peptide-based molecular electronic devices are promising due to the large diversity and unique electronic properties of biomolecules. These electronic properties can change considerably with peptide structure, allowing diverse design possibilities. In this work, we explore the effect of the side-cha...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Physical chemistry chemical physics : PCCP 2018, Vol.20 (10), p.6860-6867
Hauptverfasser: Guo, Cunlan, Sarkar, Soumyajit, Refaely-Abramson, Sivan, Egger, David A, Bendikov, Tatyana, Yonezawa, Keiichirou, Suda, Yosuke, Yamaguchi, Takuma, Pecht, Israel, Kera, Satoshi, Ueno, Nobuo, Sheves, Mordechai, Kronik, Leeor, Cahen, David
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:Peptide-based molecular electronic devices are promising due to the large diversity and unique electronic properties of biomolecules. These electronic properties can change considerably with peptide structure, allowing diverse design possibilities. In this work, we explore the effect of the side-chain of the peptide on its electronic properties, by using both experimental and computational tools to detect the electronic energy levels of two model peptides. The peptides include 2Ala and 2Trp as well as their 3-mercaptopropionic acid linker which is used to form monolayers on an Au surface. Specifically, we compare experimental ultraviolet photoemission spectroscopy measurements with density functional theory based computational results. By analyzing differences in frontier energy levels and molecular orbitals between peptides in gas-phase and in a monolayer on gold, we find that the electronic properties of the peptide side-chain are maintained during binding of the peptide to the gold substrate. This indicates that the energy barrier for the peptide electron transport can be tuned by the amino acid compositions, which suggests a route for structural design of peptide-based electronic devices.
ISSN:1463-9076
1463-9084
DOI:10.1039/c7cp08043c