ArticleScientific reports2020
Breakdown of chiral recognition of amino acids in reduced dimensions.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- All-atom protein sequence design using discrete diffusion models.Journal of cheminformatics · 2025Article
- Molecular Chiral Response Enhanced by Crosstalking Quasi-Bound States in the Continuum.ACS photonics · 2025Article
- Poly(lactide)-Based Materials Modified with Biomolecules: A Review.Materials (Basel, Switzerland) · 2024Review
- Advancements in antimicrobial nanoscale materials and self-assembling systems.Chemical Society reviews · 2022Review
- Enantioselective Discrimination of Histidine by Means of an Achiral Cubane-Bridged Bis-Porphyrin.Langmuir : the ACS journal of surfaces and colloids · 2021Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The homochirality of amino acids in living organisms is one of the great mysteries in the phenomena of life. To understand the chiral recognition of amino acids, we have used scanning tunnelling microscopy to investigate the self-assembly of molecules of the amino acid tryptophan (Trp) on Au(111). Earlier experiments showed only homochiral configurations in the self-assembly of amino acids, despite using a mixture of the two opposite enantiomers. In our study, we demonstrate that heterochiral configurations can be favored energetically when L- and D-Trp molecules are mixed to form self-assembly on the Au surface. Using density functional theory calculations, we show that the indole side chain strongly interacts with the Au surface, which reduces the system effectively to two-dimension, with chiral recognition disabled. Our study provides important insight into the recognition of the chirality of amino acid molecules in life.
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