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A minimalistic hydrolase based on co-assembled cyclic dipeptides.

Alexander J Kleinsmann1, Boris J Nachtsheim

  • 1Institut für Organische Chemie Universität Tübingen, Auf der Morgenstelle 18, 72076 Tübingen, Germany.

Organic & Biomolecular Chemistry
|December 5, 2019
PubMed
Summary

Small peptides self-assemble into stable, catalytically active aggregates. This process, crucial for understanding abiogenesis, involves histidine and cysteine cooperative behavior and C-H-π interactions for enhanced activity.

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Area of Science:

  • Biochemistry
  • Supramolecular Chemistry
  • Origin of Life Studies

Background:

  • Peptide self-assembly is fundamental to understanding abiogenesis.
  • Cyclic dipeptides (2,5-diketopiperazines - DKPs) are simple peptide structures with potential for self-assembly.

Purpose of the Study:

  • To investigate the self-assembly of DKPs with histidine, cysteine, and lipophilic amino acids.
  • To explore the catalytic activity and molecular arrangement of these peptide aggregates.

Main Methods:

  • Formation of peptide aggregates in aqueous solution.
  • Characterization of catalytic activity (esterase-like).
  • Analysis of molecular arrangement using C-H-π interactions, Hartree-Fock calculations, and 1H-NMR HRMAS NOE spectroscopy.

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Main Results:

  • Blends of DKPs with histidine/cysteine and lipophilic amino acids formed highly stable aggregates.
  • Aggregates exhibited significant esterase-like catalytic activity.
  • C-H-π interactions between specific amino acid sidechains controlled molecular arrangement and enhanced catalytic activity.

Conclusions:

  • Cooperative intermolecular behavior between histidine and cysteine drives catalytic activity in peptide aggregates.
  • C-H-π interactions are key to controlling supramolecular assembly and enhancing catalytic efficiency.
  • These findings offer insights into peptide self-assembly relevant to abiogenesis.