Sulfur Amino Acids: From Prebiotic Chemistry to Biology and Vice Versa

Youssef-Saliba, Sparta; Vallée, Yannick

doi:10.1055/a-1472-7914

Cited by 7 publications

(2 citation statements)

References 113 publications

(118 reference statements)

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“…The objective of our team was to synthesize long peptide chains in prebiotic environmental conditions. In this work, we underlined the important role of sulfur [14,15]. This has been first seen in the ability of homocysteine thiolactone 1 to react with aminonitriles (for example, aminoacetonitrile 2) to produce short chains of homocysteine containing peptides [16,17].…”

Section: Thiols In the Making Of Small Peptides And Nitrogen Heterocy...mentioning

confidence: 96%

Catalysis before Enzymes: Thiol-Rich Peptides as Molecular Diversity Providers on the Early Earth

et al. 2023

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The multiplicity of simple molecules available on the primitive Earth probably made possible the development of extremely diverse prebiotic chemistry. The importance of thiols is widely recognized in the community studying the origin of life. De Duve’s “thioester world” has been considered a major contribution in this regard, where thioester bonds have high energies and thus can contribute to several chemical reactions. Herein, we propose specific models of thiols that exhibit unique activities toward several chemical reactions. Thanks to aminothiol and aminonitrile behaviors, we were able to obtain thiol-rich peptides with interesting catalytic activities leading to the formation of structurally diverse molecules. In a broader context, such chemistry could be introduced into systems chemistry scenarios in which it would be associated with the chemistry of nucleic acids or their precursors, as well as that of fatty acids.

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Section: Thiols In the Making Of Small Peptides And Nitrogen Heterocy...mentioning

confidence: 96%

Catalysis before Enzymes: Thiol-Rich Peptides as Molecular Diversity Providers on the Early Earth

et al. 2023

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“…As they are part of iron-sulfur clusters, they are key players in the formation of metalloproteins, such as ferredoxins (four cysteine residues involved), and in zinc fingers (in which up to six cysteine units are involved), both of which are important in protein-protein and DNA (or RNA)-protein interactions. In view of the importance of thiols, the hypothesis that cysteine has been integrated into the primitive peptide chains is persuasive [18]. Plausible prebiotic syntheses of cysteine have been described [19,20].…”

Section: Introductionmentioning

confidence: 99%

Straightforward Creation of Possibly Prebiotic Complex Mixtures of Thiol-Rich Peptides

Shalayel

Leqraa

Blandin

et al. 2023

Life

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At the origin of life, extremely diverse mixtures of oligomers and polymers could be obtained from relatively simple molecular bricks. Here, we present an example of the polymerization of two amidonitriles derived from cysteine, Cys-Ala-CN and Cys-Met-CN. The thiol function in a molecule adds onto the nitrile group of another one, allowing efficient condensation reactions and making available an extensive range of polymers containing amide bonds and/or five-membered heterocycles, namely thiazolines. Macrocycles were also identified, the biggest one containing sixteen residues (cyclo(Cys-Met)8). MALDI-TOF mass spectrometry was used to identify all the present species. What these examples show is that complex mixtures are likely to have formed on the primitive Earth and that, ultimately, the selection that must have followed may have been an even more crucial step towards life than the synthesis of the pre-biological species themselves.

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Did Homocysteine Take Part in the Start of the Synthesis of Peptides on the Early Earth?

2022

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Unlike its shorter analog, cysteine, and its methylated derivative, methionine, homocysteine is not today a proteinogenic amino acid. However, this thiol containing amino acid is capable of forming an activated species intramolecularly. Its thiolactone could have made it an interesting molecular building block at the origin of life on Earth. Here we study the cyclization of homocysteine in water and show theoretically and experimentally that in an acidic medium the proportion of thiolactone is significant. This thiolactone easily reacts with amino acids to form dipeptides. We envision that these reactions may help interpret why a methionine residue is introduced at the start of all protein synthesis.

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Sulfur Amino Acids: From Prebiotic Chemistry to Biology and Vice Versa

Cited by 7 publications

References 113 publications

Catalysis before Enzymes: Thiol-Rich Peptides as Molecular Diversity Providers on the Early Earth

Catalysis before Enzymes: Thiol-Rich Peptides as Molecular Diversity Providers on the Early Earth

Straightforward Creation of Possibly Prebiotic Complex Mixtures of Thiol-Rich Peptides

Did Homocysteine Take Part in the Start of the Synthesis of Peptides on the Early Earth?

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