journal article·2026-06-03Open access

Simulation of Self-Assembled Monolayers of Polyalanine α-Helices: Development and Application of an Effective Potential for Film Structure Predictions

Hadis Ghodrati, Kevin Preis, Thi Ngoc Ha Nguyen, Christoph Tegenkamp, Sibylle Gemming, Jeffrey Kelling, Florian Günther

ACS Applied Materials & Interfaces· Volume 18· Issue 21

Abstract

Self-assembled monolayers of polyalanine α-helices exhibit distinct structural phases with implications for chiral-induced spin selectivity. We combine scanning tunneling microscopy and theoretical modeling to reveal how chiral composition governs supramolecular organization. Enantiopure systems form hexagonal lattices, while racemic mixtures organize into rectangular phases with stripe-like features. Our interaction potentials derived from density-functional based tight binding calculations show that opposite-handed helix pairs exhibit stronger binding and closer packing, explaining the denser racemic structures. Crucially, we demonstrate that the observed STM contrast arises from antiparallel alignment of opposite-handed helices rather than physical height variations. These findings establish fundamental structure-property relationships for designing peptide-based spintronic materials.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Synthesis and Properties of Aromatic Compounds · Block Copolymer Self-Assembly · Surface Chemistry and Catalysis

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Institute of Physics

Technische Universität Chemnitz

Institute for Radiation Physics

Helmholtz-Zentrum Dresden - Rossendorf

Departamento de Física Instituto de Geociências e Ciências Exatas

Universidade Estadual Paulista

Funding

Deutsche Forschungsgemeinschaft · Conselho Nacional de Desenvolvimento Cient?fico e Tecnol?gico · Funda??o de Amparo ? Pesquisa do Estado de S?o Paulo

References (30)

Show source-provided references
1. 10.1016/j.actbio.2009.01.01610.1016/j.actbio.2009.01.016 ↗
2. 10.1038/pj.2013.2710.1038/pj.2013.27 ↗
3. 10.1126/science.aar426510.1126/science.aar4265 ↗
4. 10.1021/acs.chemrev.3c0066110.1021/acs.chemrev.3c00661 ↗
5. 10.1038/nature1982010.1038/nature19820 ↗
6. 10.1146/annurev-physchem-082423-03293310.1146/annurev-physchem-082423-032933 ↗
7. 10.1039/D0TC02734K10.1039/D0TC02734K ↗
8. 10.1021/jp052157p10.1021/jp052157p ↗
9. 10.1021/bi963015b10.1021/bi963015b ↗
10. 10.1021/acs.jpclett.9b0348710.1021/acs.jpclett.9b03487 ↗
11. 10.1126/sciadv.ado428510.1126/sciadv.ado4285 ↗
12. 10.1021/acs.nanolett.4c0038310.1021/acs.nanolett.4c00383 ↗
13. 10.1021/acs.jpcc.8b1062010.1021/acs.jpcc.8b10620 ↗
14. 10.1021/acs.jpcc.0c0363110.1021/acs.jpcc.0c03631 ↗
15. 10.1126/science.adk563410.1126/science.adk5634 ↗
16. 10.1002/smll.20230823310.1002/smll.202308233 ↗
17. 10.1021/acs.jpclett.5c0075510.1021/acs.jpclett.5c00755 ↗
18. 10.1021/ja049298+10.1021/ja049298+ ↗
19. 10.1039/C6CP03827A10.1039/C6CP03827A ↗
20. 10.1126/science.223741510.1126/science.2237415 ↗
21. 10.1021/acsami.3c0142910.1021/acsami.3c01429 ↗
22. 10.1002/jlac.1895286010510.1002/jlac.18952860105 ↗
23. 10.1021/acs.jpcc.0c0024610.1021/acs.jpcc.0c00246 ↗
24. 10.1039/D4SC04435E10.1039/D4SC04435E ↗
25. 10.1103/PhysRevB.58.726010.1103/PhysRevB.58.7260 ↗
26. 10.1063/1.514319010.1063/1.5143190 ↗
27. 10.1021/ja00051a04010.1021/ja00051a040 ↗
28. 10.1021/acs.chemrev.5b0058410.1021/acs.chemrev.5b00584 ↗
29. 10.1021/acs.jcim.5c0040110.1021/acs.jcim.5c00401 ↗
30. 10.1016/S0009-2614(99)01201-410.1016/S0009-2614(99)01201-4 ↗