Abiotic Acyl Transfer Cascades Driven by Aminoacyl Phosphate Esters and Self-Assembly DOI Creative Commons
Mahesh D. Pol, Ralf Thomann, Yi Thomann

et al.

Journal of the American Chemical Society, Journal Year: 2024, Volume and Issue: 146(43), P. 29621 - 29629

Published: Oct. 17, 2024

Biochemical acyl transfer cascades, such as those initiated by the adenylation of carboxylic acids, are central to various biological processes, including protein synthesis and fatty acid metabolism. Designing cascade reactions in aqueous media remains challenging due need control multiple, sequential a single pot manage stability reactive intermediates. Herein, we developed abiotic cascades using aminoacyl phosphate esters, synthetic counterparts adenylates, drive chemical self-assembly pot. We demonstrated that structural elements amino side chains (aromatic versus aliphatic) significantly influence reactivity half-lives ranging from hours days. This behavior, turn, affects number couplings can achieve network propensity activated intermediate structures. The constructed bifunctional peptide substrates featuring chain nucleophiles. Specifically, aromatic acids facilitate formation transient thioesters, which preorganized into spherical aggregates further couple chimeric assemblies composed esters thioesters. In contrast, aliphatic lack ability form structures, predominantly undergo hydrolysis, bypassing transformations after thioester formation. Additionally, mixtures containing multiple substrates, achieved selective product following distinct pathway favors subsequent through changes self-assembly. By coupling with molecules varying time scales, reaction clocks lifetimes dynamics, facilitating precise temporal regulation.

Language: Английский

Abiotic Acyl Transfer Cascades Driven by Aminoacyl Phosphate Esters and Self-Assembly DOI Creative Commons
Mahesh D. Pol, Ralf Thomann, Yi Thomann

et al.

Journal of the American Chemical Society, Journal Year: 2024, Volume and Issue: 146(43), P. 29621 - 29629

Published: Oct. 17, 2024

Biochemical acyl transfer cascades, such as those initiated by the adenylation of carboxylic acids, are central to various biological processes, including protein synthesis and fatty acid metabolism. Designing cascade reactions in aqueous media remains challenging due need control multiple, sequential a single pot manage stability reactive intermediates. Herein, we developed abiotic cascades using aminoacyl phosphate esters, synthetic counterparts adenylates, drive chemical self-assembly pot. We demonstrated that structural elements amino side chains (aromatic versus aliphatic) significantly influence reactivity half-lives ranging from hours days. This behavior, turn, affects number couplings can achieve network propensity activated intermediate structures. The constructed bifunctional peptide substrates featuring chain nucleophiles. Specifically, aromatic acids facilitate formation transient thioesters, which preorganized into spherical aggregates further couple chimeric assemblies composed esters thioesters. In contrast, aliphatic lack ability form structures, predominantly undergo hydrolysis, bypassing transformations after thioester formation. Additionally, mixtures containing multiple substrates, achieved selective product following distinct pathway favors subsequent through changes self-assembly. By coupling with molecules varying time scales, reaction clocks lifetimes dynamics, facilitating precise temporal regulation.

Language: Английский

Citations

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