ArticleThe journal of physical chemistry. B2021
Binding of Dipeptides to Fatty Acid Membranes Explains Their Colocalization in Protocells but Does Not Select for Them Relative to Unjoined Amino Acids.
Article in The journal of physical chemistry. B, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Growth of fatty acid vesicles coupled with amino acid sequences of peptides toward evolvable protocells.Communications chemistry · 2026Article
- Prebiotic Peptide Synthesis: How Did Longest Peptide Appear?Journal of molecular evolution · 2025Review
- Plausible Sources of Membrane-Forming Fatty Acids on the Early Earth: A Review of the Literature and an Estimation of Amounts.ACS earth & space chemistry · 2023Review
- DNA and the origins of life in micaceous clay.Biophysical journal · 2022Article
- Spontaneous Formation of Functional Structures in Messy Environments.Life (Basel, Switzerland) · 2022Article
- Scum of the Earth: A Hypothesis for Prebiotic Multi-Compartmentalised Environments.Life (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Dipeptides, which consist of two amino acids joined by a peptide bond, have been shown to have catalytic functions. This observation leads to fundamental questions relevant to the origin of life. How could peptides have become colocalized with the first protocells? Which structural features would have determined the association of amino acids and peptides with membranes? Could the association of dipeptides with protocell membranes have driven molecular evolution, favoring dipeptides over individual amino acids? Using pulsed-field gradient nuclear magnetic resonance, we find that several prebiotic amino acids and dipeptides bind to prebiotic membranes. For amino acids, the side chains and carboxylate contribute to the interaction. For dipeptides, the extent of binding is generally less than that of the constituent amino acids, implying that other mechanisms would be necessary to drive molecular evolution. Nevertheless, our results are consistent with a scheme in which the building blocks of the biological polymers colocalized with protocells prior to the emergence of RNA and proteins.
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Registered trials
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