ArticleOrigins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life1999
Mutual amino acid catalysis in salt-induced peptide formation supports this mechanism's role in prebiotic peptide evolution.
Article in Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life, 1999. 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, 34 citations in OpenAlex.
- The RNA-Binding Function of Ribosomal Proteins and Ribosome Biogenesis Factors in Human Health and Disease.Biomedicines · 2023Review
- Hydrothermal Microflow Technology as a Research Tool for Origin-of-Life Studies in Extreme Earth Environments.Life (Basel, Switzerland) · 2017Review
- Small and Random Peptides: An Unexplored Reservoir of Potentially Functional Primitive Organocatalysts. The Case of Seryl-Histidine.Life (Basel, Switzerland) · 2017Review
- One-step formation of oligopeptide-like molecules from Glu and Asp in hydrothermal environments.Die Naturwissenschaften · 2008Article
- Amino acid interaction with and adsorption on clays: FT-IR and Mössbauer spectroscopy and X-ray diffractometry investigations.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2007Article
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2 authors at 1 institution in 1 country.
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Abstract
The presence of some amino acids and dipeptides under the conditions of the salt-induced peptide formation reaction (aqueous solution at 85 degrees C, Cu(II) and NaCl) has been found to catalyze the formation of homopeptides of other amino acids, which are otherwise produced only in traces or not at all by this reaction. The condensation of Val, Leu and Lys to form their homodipeptides can occur to a considerable extent due to catalytic effects of other amino acids and related compounds, among which glycine, histidine, diglycine and diketopiperazine exhibit the most remarkable activity. These findings also lead to a modification of the table of amino acid sequences preferentially formed by the salt-induced peptide formation (SIPF) reaction, previously used for a comparison with the sequence preferences in membrane proteins of primitive organisms.
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