Self-assembly of L-methionine on Cu(111): Steering chiral organization by substrate reactivity and thermal activation

Agustin Eduardo Schiffrin, Joachim Reichert, Yan Pennec, Wilhelm Auwarter, Alexander Weber-Bargioni, Matthias Marschall, Martina Dell'Angela, Dean Cvetko, Gregor Bavdek, Albano Cossaro, Alberto Morgante, Johannes V Barth

Research output: Contribution to journalArticleResearchpeer-review

Abstract

The self-assembly of the amino acid L-methionine on Cu(111) was investigated under ultrahigh vacuum (UHV) conditions by scanning tunneling microscopy (STM), helium atom scattering (HAS) and X-ray photoelectron spectroscopy (XPS). The system is strongly influenced by the substrate reactivity and the deposition temperature. The STM and HAS structural analysis yields that, for temperatures below 273 K, the biomolecules assemble in strings oriented with an angle of -10 degrees with respect to the (110) axes of the substrate. For temperatures above 283 K, a regular and ordered one-dimensional (1D) phase arises following an angle of +10 degrees with respect to the same directions. High resolution STM data of this ordered 1D arrangement evidence molecular dimerization and dimer alignment into ordered chains which are commensurate with the Cu(111) atomic lattice. XPS measurements reveal that the high temperature ordered phase consists of an exclusively anionic ensemble with a deprotonated carboxylic group and a neutral amino group, while the low temperature phase is heterogeneously composed of both zwitterionic and anionic species, depending on whether the molecules are immobilized in clusters of dimers on the free terraces or at the low-coordinated adsorption sites of the substrate step-edges. These combined results evidence a structural transformation of the supramolecular assembly which is triggered by a thermally activated process involving the underlying Cu(111) substrate and which carries the intrinsic chiral signature of the adsorbed molecular units
Original languageEnglish
Pages (from-to)12101 - 12108
Number of pages8
JournalJournal of Physical Chemistry C
Volume113
Issue number28
DOIs
Publication statusPublished - 2009
Externally publishedYes

Cite this

Schiffrin, Agustin Eduardo ; Reichert, Joachim ; Pennec, Yan ; Auwarter, Wilhelm ; Weber-Bargioni, Alexander ; Marschall, Matthias ; Dell'Angela, Martina ; Cvetko, Dean ; Bavdek, Gregor ; Cossaro, Albano ; Morgante, Alberto ; Barth, Johannes V. / Self-assembly of L-methionine on Cu(111): Steering chiral organization by substrate reactivity and thermal activation. In: Journal of Physical Chemistry C. 2009 ; Vol. 113, No. 28. pp. 12101 - 12108.
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title = "Self-assembly of L-methionine on Cu(111): Steering chiral organization by substrate reactivity and thermal activation",
abstract = "The self-assembly of the amino acid L-methionine on Cu(111) was investigated under ultrahigh vacuum (UHV) conditions by scanning tunneling microscopy (STM), helium atom scattering (HAS) and X-ray photoelectron spectroscopy (XPS). The system is strongly influenced by the substrate reactivity and the deposition temperature. The STM and HAS structural analysis yields that, for temperatures below 273 K, the biomolecules assemble in strings oriented with an angle of -10 degrees with respect to the (110) axes of the substrate. For temperatures above 283 K, a regular and ordered one-dimensional (1D) phase arises following an angle of +10 degrees with respect to the same directions. High resolution STM data of this ordered 1D arrangement evidence molecular dimerization and dimer alignment into ordered chains which are commensurate with the Cu(111) atomic lattice. XPS measurements reveal that the high temperature ordered phase consists of an exclusively anionic ensemble with a deprotonated carboxylic group and a neutral amino group, while the low temperature phase is heterogeneously composed of both zwitterionic and anionic species, depending on whether the molecules are immobilized in clusters of dimers on the free terraces or at the low-coordinated adsorption sites of the substrate step-edges. These combined results evidence a structural transformation of the supramolecular assembly which is triggered by a thermally activated process involving the underlying Cu(111) substrate and which carries the intrinsic chiral signature of the adsorbed molecular units",
author = "Schiffrin, {Agustin Eduardo} and Joachim Reichert and Yan Pennec and Wilhelm Auwarter and Alexander Weber-Bargioni and Matthias Marschall and Martina Dell'Angela and Dean Cvetko and Gregor Bavdek and Albano Cossaro and Alberto Morgante and Barth, {Johannes V}",
year = "2009",
doi = "10.1021/jp900593g",
language = "English",
volume = "113",
pages = "12101 -- 12108",
journal = "Journal of Physical Chemistry C",
issn = "1932-7447",
publisher = "American Chemical Society",
number = "28",

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Schiffrin, AE, Reichert, J, Pennec, Y, Auwarter, W, Weber-Bargioni, A, Marschall, M, Dell'Angela, M, Cvetko, D, Bavdek, G, Cossaro, A, Morgante, A & Barth, JV 2009, 'Self-assembly of L-methionine on Cu(111): Steering chiral organization by substrate reactivity and thermal activation' Journal of Physical Chemistry C, vol. 113, no. 28, pp. 12101 - 12108. https://doi.org/10.1021/jp900593g

Self-assembly of L-methionine on Cu(111): Steering chiral organization by substrate reactivity and thermal activation. / Schiffrin, Agustin Eduardo; Reichert, Joachim; Pennec, Yan; Auwarter, Wilhelm; Weber-Bargioni, Alexander; Marschall, Matthias; Dell'Angela, Martina; Cvetko, Dean; Bavdek, Gregor; Cossaro, Albano; Morgante, Alberto; Barth, Johannes V.

In: Journal of Physical Chemistry C, Vol. 113, No. 28, 2009, p. 12101 - 12108.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Self-assembly of L-methionine on Cu(111): Steering chiral organization by substrate reactivity and thermal activation

AU - Schiffrin, Agustin Eduardo

AU - Reichert, Joachim

AU - Pennec, Yan

AU - Auwarter, Wilhelm

AU - Weber-Bargioni, Alexander

AU - Marschall, Matthias

AU - Dell'Angela, Martina

AU - Cvetko, Dean

AU - Bavdek, Gregor

AU - Cossaro, Albano

AU - Morgante, Alberto

AU - Barth, Johannes V

PY - 2009

Y1 - 2009

N2 - The self-assembly of the amino acid L-methionine on Cu(111) was investigated under ultrahigh vacuum (UHV) conditions by scanning tunneling microscopy (STM), helium atom scattering (HAS) and X-ray photoelectron spectroscopy (XPS). The system is strongly influenced by the substrate reactivity and the deposition temperature. The STM and HAS structural analysis yields that, for temperatures below 273 K, the biomolecules assemble in strings oriented with an angle of -10 degrees with respect to the (110) axes of the substrate. For temperatures above 283 K, a regular and ordered one-dimensional (1D) phase arises following an angle of +10 degrees with respect to the same directions. High resolution STM data of this ordered 1D arrangement evidence molecular dimerization and dimer alignment into ordered chains which are commensurate with the Cu(111) atomic lattice. XPS measurements reveal that the high temperature ordered phase consists of an exclusively anionic ensemble with a deprotonated carboxylic group and a neutral amino group, while the low temperature phase is heterogeneously composed of both zwitterionic and anionic species, depending on whether the molecules are immobilized in clusters of dimers on the free terraces or at the low-coordinated adsorption sites of the substrate step-edges. These combined results evidence a structural transformation of the supramolecular assembly which is triggered by a thermally activated process involving the underlying Cu(111) substrate and which carries the intrinsic chiral signature of the adsorbed molecular units

AB - The self-assembly of the amino acid L-methionine on Cu(111) was investigated under ultrahigh vacuum (UHV) conditions by scanning tunneling microscopy (STM), helium atom scattering (HAS) and X-ray photoelectron spectroscopy (XPS). The system is strongly influenced by the substrate reactivity and the deposition temperature. The STM and HAS structural analysis yields that, for temperatures below 273 K, the biomolecules assemble in strings oriented with an angle of -10 degrees with respect to the (110) axes of the substrate. For temperatures above 283 K, a regular and ordered one-dimensional (1D) phase arises following an angle of +10 degrees with respect to the same directions. High resolution STM data of this ordered 1D arrangement evidence molecular dimerization and dimer alignment into ordered chains which are commensurate with the Cu(111) atomic lattice. XPS measurements reveal that the high temperature ordered phase consists of an exclusively anionic ensemble with a deprotonated carboxylic group and a neutral amino group, while the low temperature phase is heterogeneously composed of both zwitterionic and anionic species, depending on whether the molecules are immobilized in clusters of dimers on the free terraces or at the low-coordinated adsorption sites of the substrate step-edges. These combined results evidence a structural transformation of the supramolecular assembly which is triggered by a thermally activated process involving the underlying Cu(111) substrate and which carries the intrinsic chiral signature of the adsorbed molecular units

UR - http://pubs.acs.org/doi/pdf/10.1021/jp900593g

U2 - 10.1021/jp900593g

DO - 10.1021/jp900593g

M3 - Article

VL - 113

SP - 12101

EP - 12108

JO - Journal of Physical Chemistry C

JF - Journal of Physical Chemistry C

SN - 1932-7447

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