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Bioorthogonal Aza-Michael Addition to Dehydrated Amino Acids in Antimicrobial Peptides

26 December 2023, Version 1
Working Paper
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

We report the efficient and site selective modification of non-canonical dehydroamino acids in ribosomally synthesized and post-transationally modified peptides (RiPPs) by β-amination. The singly modified thiopeptide Thiostrepton showed an up to 35-fold increase in water solubility, and minimum inhibitory concentration (MIC) assays showed that antimicrobial activity was maintained.

Keywords

bioorthogonal chemistry
aza-Michael addition
thiostrepton
nisin
RiPPs

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Version History

Dec 26, 2023 Version 1

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The content is available under CC BY NC ND 4.0 [opens in a new tab]

DOI

10.26434/chemrxiv-2023-16rwj
D O I: 10.26434/chemrxiv-2023-16rwj [opens in a new tab]

Funding

Ministerie van Onderwijs, Cultuur en Wetenschap
024.001.035

Author’s competing interest statement

The author(s) have declared they have no conflict of interest with regard to this content

Ethics

The author(s) have declared ethics committee/IRB approval is not relevant to this content

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