Search for catalytic properties of simple polypeptides

Barbier, Bernard; Brack, Andrè

doi:10.1007/bf02386476

Cited by 18 publications

(7 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…From a systematic study run in our laboratory, no significant effects have been found, so far. More interestingly, basic polypeptides strongly accelerate the hydrolysis of oligoadenylates [26]. Attempts to reverse the reaction are currently being undertaken in our group.…”

Section: Resultsmentioning

confidence: 99%

Selective emergence and survival of early polypeptides in water

Brack

1987

Origins Life Evol Biosphere

View full text Add to dashboard Cite

Oligopeptides essential to primitive cells could not be obtained just by raising the background noise of organic compounds produced by a prebiotic chemistry working at random. Selection pathways were required. Experimental evidence is given for selective condensation of amino acids in water as well as for selective resistance to degradation. It is shown that N-carboxyanhydrides are good candidates for chemical selection in water. They are formed when active esters of amino acids are left in the presence of bicarbonate ions or when N,N'-carbonyldiimidazole is used as condensing agent. Polymerization of a mixture of proteinaceous and non-proteinaceous amino acids leads to an enrichment in the proteinaceous ones plus alpha-aminobutyric acid. Selective resistance toward degradation of beta-pleated sheet conformation is used to exemplify a possible accumulation of homochiral sequences made of hydrophilic and strong hydrophobic residues. Amino acids with branched aliphatic side-chains are selected but those having short linear aliphatic side-chains such as alpha-aminobutyric acid or norvaline are not.

show abstract

Section: Resultsmentioning

confidence: 99%

Selective emergence and survival of early polypeptides in water

Brack

1987

Origins Life Evol Biosphere

View full text Add to dashboard Cite

show abstract

“…An additional question ensuing from their abiotic formation is that of the potential role that the peptides could have played in the origin of life process. The ones that bear functional sidechain groups could be involved in catalytic activities or association with other components by hydrogen bonding or covalent interactions but any property resulting from the formation of tridimensional structures required much longer sequences (Barbier and Brack 1987;Luisi 2007). Moreover, the stability of peptide bonds is limited, as shown by apparent equilibrium constant values of c.a.…”

Section: Introductionmentioning

confidence: 98%

The Activation of Free Dipeptides Promoted by Strong Activating Agents in Water Does not Yield Diketopiperazines

Beaufils

Jepaul

Liu

et al. 2015

Orig Life Evol Biosph

View full text Add to dashboard Cite

The activation of dipeptides was studied in the perspective of the abiotic formation of oligopeptides of significant length as a requirement for secondary structure formation. The formation of piperazin-2,5-diones (DKP), previously considered as a dead end when activating free dipeptides, was shown in this work to be efficiently suppressed when using strong activating agents (e.g., carbodiimides). This behaviour was explained by the fast formation of a 5(4H)-oxazolone intermediate at a rate that exceeds the time scale of the rotation of the peptide bond from the predominant trans-conformation into the cis-isomer required for DKP formation. No DKP was observed when using strong activating agents whereas phosphate mixed anhydrides or moderately activated esters were observed to predominantly yield DKP. The DKP side-reaction no longer constitutes a drawback for the C-terminus elongation of peptides. These results are considered as additional evidence that pathways involving strong activation are required to drive the emergence of living entities rather than close to equilibrium processes.

show abstract

“…427 On the other hand, poly(Leu-Lys) was also found to promote the oligomerization of activated mononucleotide diphosphates, being especially effective in increasing the abundance of longer oligomers. 430,431 The cleavage of ribonucleotides was promoted by a set of 12-mer or 20-mer peptides that were enriched in Lys or His, especially in the presence of certain divalent metal ions; 432 in contrast, an analogous Arg-rich 20-mer peptide did not promote RNA cleavage. 433 In contrast to the above studies, a dinucleotide was protected from metal-ion-mediated hydrolysis by thermal copolymers of Gly, Ala, Glu, Asp, and His.…”

Section: Peptide Interactions With Nucleic Acidsmentioning

confidence: 99%

Prebiotic Peptides: Molecular Hubs in the Origin of Life

et al. 2020

View full text Add to dashboard Cite

The fundamental roles that peptides and proteins play in today’s biology makes it almost indisputable that peptides were key players in the origin of life. Insofar as it is appropriate to extrapolate back from extant biology to the prebiotic world, one must acknowledge the critical importance that interconnected molecular networks, likely with peptides as key components, would have played in life’s origin. In this review, we summarize chemical processes involving peptides that could have contributed to early chemical evolution, with an emphasis on molecular interactions between peptides and other classes of organic molecules. We first summarize mechanisms by which amino acids and similar building blocks could have been produced and elaborated into proto-peptides. Next, non-covalent interactions of peptides with other peptides as well as with nucleic acids, lipids, carbohydrates, metal ions, and aromatic molecules are discussed in relation to the possible roles of such interactions in chemical evolution of structure and function. Finally, we describe research involving structural alternatives to peptides and covalent adducts between amino acids/peptides and other classes of molecules. We propose that ample future breakthroughs in origin-of-life chemistry will stem from investigations of interconnected chemical systems in which synergistic interactions between different classes of molecules emerge.

show abstract

Search for catalytic properties of simple polypeptides

Cited by 18 publications

References 24 publications

Selective emergence and survival of early polypeptides in water

Selective emergence and survival of early polypeptides in water

The Activation of Free Dipeptides Promoted by Strong Activating Agents in Water Does not Yield Diketopiperazines

Prebiotic Peptides: Molecular Hubs in the Origin of Life

Contact Info

Product

Resources

About