Pathways for the formation and evolution of peptides in prebiotic environments

Danger, Grégoire; Plasson, Raphaël; Pascal, Robert

doi:10.1039/c2cs35064e

Cited by 172 publications

(178 citation statements)

References 114 publications

(152 reference statements)

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“…The originality of this pathway lies in BIO Web of Conferences 04001-p. 4 the fact that peptide coupling is associated with a high level epimerization at the C-terminal residue. This change of configuration at a selected position in the peptide suggests that a reproduction of chirality is possible at the same time as peptide elongation proceeds, which is worth of being studied more deeply because of its possible consequences on the emergence of homochirality that could take place in a way similar to the APED model [18], which would require a protometabolism of peptide based on C-terminus elongation to be established ( Figure 5). …”

Section: Cyanamidementioning

confidence: 99%

“…Although 5(4H)-oxazolone are well known to induce racemization in aqueous solution, their intermediacy improving peptide coupling in aqueous solution needed to be demonstrated. Information establishing this pathway have been obtained [21], which definitely shows that Cterminal elongation is a prebiotically relevant pathway [18]. The originality of this pathway lies in BIO Web of Conferences 04001-p. 4 the fact that peptide coupling is associated with a high level epimerization at the C-terminal residue.…”

Section: Cyanamidementioning

confidence: 99%

“…This has been demonstrated in the case of α-amino acid N-carboxyanhydrides leading to mixed anhydrides reminiscent of aminoacyl adenylates by interaction with phosphates and nucleotides [41][42][43] ( Figure 6). 5(4H)-Oxazolone are likely to give similar mixed anhydrides and the corresponding downhill less activated products with a large variety of chemical pathways that may be conceived [18]. …”

Section: Epov 2012mentioning

confidence: 99%

“…The new and improbable properties emerging this kind of processes are the object of study of Systems Chemistry [16,17]. We report here on the conceptual background leading our studies [18] and on the results of studies carried out to assess the possibilities of a potential Systems Chemistry of α-amino acids and peptides [19][20][21].…”

Section: Introductionmentioning

confidence: 99%

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Systems chemistry of α-amino acids and peptides

Danger

Boiteau

Rossi

et al. 2014

BIO Web of Conferences

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Abstract.Pathways have been disclosed in the past decade, which support the possibility that α-amino acids could have contributed to self-organization processes leading to the emergence of life. It is proposed that the systems chemistry of these simple building blocks may have led to features of self-organization through the realization of protometabolisms based on unidirectional loops involving both peptide formation and breakdown and additional feedback processes. Potential peptide activating agents have been identified. Scenarios of peptide elongation are proposed to account for peptide elongation both at the N-terminus and the C-terminus and new indications that these processes could be involved in symmetry breaking have been provided.

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Section: Cyanamidementioning

confidence: 99%

Section: Cyanamidementioning

confidence: 99%

Section: Epov 2012mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Systems chemistry of α-amino acids and peptides

Danger

Boiteau

Rossi

et al. 2014

BIO Web of Conferences

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“…As a result of this staggering number, progress on the characterization of plausibly prebiotic amino acid pools (1,13,(21)(22)(23)(24)(25), abiotic mechanisms for peptide selfassembly (10,(26)(27)(28)(29)(30), and the evolution of early ribosomes (31,32) has not been paralleled by a systems-level understanding of proto-peptide diversity.…”

mentioning

confidence: 99%

Surveying the sequence diversity of model prebiotic peptides by mass spectrometry

Forsythe

Petrov

Millar

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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The rise of peptides with secondary structures and functions would have been a key step in the chemical evolution which led to life. As with modern biology, amino acid sequence would have been a primary determinant of peptide structure and activity in an originsof-life scenario. It is a commonly held hypothesis that unique functional sequences would have emerged from a diverse soup of proto-peptides, yet there is a lack of experimental data in support of this. Whereas the majority of studies in the field focus on peptides containing only one or two types of amino acids, here we used modern mass spectrometry (MS)-based techniques to separate and sequence de novo proto-peptides containing broader combinations of prebiotically plausible monomers. Using a dry-wet environmental cycling protocol, hundreds of proto-peptide sequences were formed over a mere 4 d of reaction. Sequence homology diagrams were constructed to compare experimental and theoretical sequence spaces of tetrameric proto-peptides. MS-based analyses such as this will be increasingly necessary as origins-of-life researchers move toward systems-level investigations of prebiotic chemistry. . Soon after, Fox and Harada began to explore the formation of peptides from amino acids via condensation at high temperatures (2). These reactions were facilitated by proportionally higher concentrations of amino acids with acidic side chains (e.g., aspartic acid, D) and resulted in the production of "proteinoids," condensation products containing covalent cross-links not found in coded proteins. In their 1960 manuscript, Fox and Harada speculated about the diversity of proteinoid sequences, yet conceded that "a complete answer to the question of whether the amino acid residues are distributed in a random or other arrangement may require a complete assignment of residues in one molecular species," a task beyond the analytical capabilities of the time (3).In subsequent years, the proteinoid concept was displaced by the hypothesis that either RNA or proto-RNA gave rise to life (4-6). Nevertheless, to this day, condensation reactions of amino acids are thought to have played a key role in a potentially symbiotic proto-nucleic acid and proto-peptide world (7,8). Peptide condensation studies at temperatures lower than those of Fox and Harada, or with the aid of chemical agents, confirmed that abiotic production of peptides was indeed possible, but chain lengths were generally limited to dimers and trimers with low yields (9). In recent studies, this length barrier has been surpassed, and certain proto-peptides have been shown to form aggregate structures (10, 11). Nevertheless, the majority of proto-peptide studies have been limited in scope, typically containing only one or two types of amino acid monomer.We recently introduced a model prebiotic pathway for peptide formation based on ester-amide exchange reactions between α-amino acids and α-hydroxy acids (12), amino acid structural analogs found in meteorites and model prebiotic reactions (13, 14) (Fig. 1A). Subjecting ...

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The ambivalent role of water at the origins of life

et al. 2020

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Life as we know it would not exist without water. However, water molecules not only serve as a solvent and reactant but can also promote hydrolysis, which counteracts the formation of essential organic molecules. This conundrum constitutes one of the central issues in origin of life. Hydrolysis is an important part of energy metabolism for all living organisms but only because, inside cells, it is a controlled reaction. How could hydrolysis have been regulated under prebiotic settings? Lower water activities possibly provide an answer: geochemical sites with less free and more bound water can supply the necessary conditions for protometabolic reactions. Such conditions occur in serpentinising systems, hydrothermal sites that synthesise hydrogen gas via rock–water interactions. Here, we summarise the parallels between biotic and abiotic means of controlling hydrolysis in order to narrow the gap between biochemical and geochemical reactions and briefly outline how hydrolysis could even have played a constructive role at the origin of molecular self‐organisation.

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Pathways for the formation and evolution of peptides in prebiotic environments

Cited by 172 publications

References 114 publications

Systems chemistry of α-amino acids and peptides

Systems chemistry of α-amino acids and peptides

Surveying the sequence diversity of model prebiotic peptides by mass spectrometry

The ambivalent role of water at the origins of life

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