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Mutually stabilizing interactions between proto-peptides and RNA.

Moran Frenkel-Pinter1,2,3, Jay W Haynes1,2, Ahmad M Mohyeldin1,2

  • 1NSF/NASA Center for Chemical Evolution, Atlanta, GA, USA.

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|June 21, 2020
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Summary
This summary is machine-generated.

Early peptides and RNA mutually stabilized each other, suggesting a co-evolutionary history. Cationic proto-peptides enhanced RNA thermal stability and RNA extended proto-peptide lifetime, supporting early interdependence.

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Area of Science:

  • Origin of life studies
  • Biochemistry
  • Molecular evolution

Background:

  • The synergy between peptides and nucleic acids in modern biology suggests functional co-evolution.
  • Understanding early molecular interactions is key to deciphering life's origins.

Purpose of the Study:

  • To investigate the direct interactions between cationic proto-peptides and RNA.
  • To determine if these interactions lead to mutual stabilization and provide insights into early molecular co-evolution.

Main Methods:

  • Synthetically prepared or prebiotically derived cationic proto-peptides (depsipeptides and polyesters) were used.
  • Interactions with RNA were studied, focusing on thermal stability and molecular lifetime.
  • The role of specific amino acids (Lys, Arg, His) in proto-peptides was examined.

Main Results:

  • Cationic proto-peptides directly interacted with and stabilized RNA structures.
  • Proto-peptides significantly increased the thermal stability of folded RNA.
  • RNA extended the lifetime of a depsipeptide by over 30-fold.
  • Proteinaceous amino acids in proto-peptides enhanced RNA duplex thermal stability more than non-proteinaceous ones.

Conclusions:

  • The findings support a model of co-evolution between early polypeptides and nucleic acids.
  • Rudimentary, mutually stabilizing interactions likely occurred at the dawn of peptide and nucleic acid co-existence.
  • This early interdependence laid the groundwork for the complex RNA-protein synergy seen today.