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A minimalistic hydrolase based on co-assembled cyclic dipeptides

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Abstract

The self-assembly of small peptides into larger aggregates is an important process for the fundamental understanding of abiogenesis. In this article we demonstrate that blends of cyclic dipeptides (2,5-diketopiperazines – DKPs) bearing either histidine or cysteine in combination with a lipophilic amino acid form highly stable aggregates in aqueous solution with esterase-like activity. We demonstrate that the catalytic activity is based on an intermolecular cooperative behavior between histidine and cysteine. A high control of the molecular arrangement of the peptide assemblies was gained by C–H-π interactions between Phe and Leu or Val sidechains, resulting in a significant increase in catalytic activity. These interactions were strongly supported by Hartree–Fock calculations and finally confirmed via 1H-NMR HRMAS NOE spectroscopy.

Graphical abstract: A minimalistic hydrolase based on co-assembled cyclic dipeptides

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Publication details

The article was received on 10 Oct 2019, accepted on 25 Nov 2019 and first published on 26 Nov 2019


Article type: Paper
DOI: 10.1039/C9OB02198A
Org. Biomol. Chem., 2020, Advance Article

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    A minimalistic hydrolase based on co-assembled cyclic dipeptides

    A. J. Kleinsmann and B. J. Nachtsheim, Org. Biomol. Chem., 2020, Advance Article , DOI: 10.1039/C9OB02198A

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