Selective Aza-Michael Addition to Dehydrated Amino Acids in Natural Antimicrobial Peptides

Michela Vargiu; Yanli Xu; Oscar Kuipers; Gerard Roelfes

doi:10.1002/cbic.202400043

Selective Aza-Michael Addition to Dehydrated Amino Acids in Natural Antimicrobial Peptides

Michela Vargiu, Yanli Xu, Oscar Kuipers, Gerard Roelfes^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

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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 remained good, albeit lower than the unmodified peptide. Also the lanthipeptide nisin could be modified using this method.

Original language	English
Article number	e202400043
Number of pages	5
Journal	ChemBioChem
Volume	25
Issue number	7
Early online date	28-Feb-2024
DOIs	https://doi.org/10.1002/cbic.202400043
Publication status	Published - 2-Apr-2024

Keywords

site-selective
antimicrobial peptides
Thiostrepton
Nisin
aza-michael

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Selective Aza‐Michael Addition to Dehydrated Amino Acids in Natural Antimicrobial PeptidesProof, 1.91 MBLicence: CC BY

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title = "Selective Aza-Michael Addition to Dehydrated Amino Acids in Natural Antimicrobial Peptides",

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 remained good, albeit lower than the unmodified peptide. Also the lanthipeptide nisin could be modified using this method.",

keywords = "site-selective, antimicrobial peptides, Thiostrepton, Nisin, aza-michael",

author = "Michela Vargiu and Yanli Xu and Oscar Kuipers and Gerard Roelfes",

note = "{\textcopyright} 2024 Wiley-VCH GmbH.",

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TY - JOUR

T1 - Selective Aza-Michael Addition to Dehydrated Amino Acids in Natural Antimicrobial Peptides

AU - Vargiu, Michela

AU - Xu, Yanli

AU - Kuipers, Oscar

AU - Roelfes, Gerard

PY - 2024/4/2

Y1 - 2024/4/2

N2 - 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 remained good, albeit lower than the unmodified peptide. Also the lanthipeptide nisin could be modified using this method.

AB - 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 remained good, albeit lower than the unmodified peptide. Also the lanthipeptide nisin could be modified using this method.

KW - site-selective

KW - antimicrobial peptides

KW - Thiostrepton

KW - Nisin

KW - aza-michael

U2 - 10.1002/cbic.202400043

DO - 10.1002/cbic.202400043

M3 - Article

C2 - 38334959

SN - 1439-4227

VL - 25

JO - ChemBioChem

JF - ChemBioChem

IS - 7

M1 - e202400043

ER -

Selective Aza-Michael Addition to Dehydrated Amino Acids in Natural Antimicrobial Peptides

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