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 voor dit werk

Onderzoeksoutput › Academic › peer review

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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.

Originele taal-2	English
Artikelnummer	e202400043
Aantal pagina's	5
Tijdschrift	ChemBioChem
Volume	25
Nummer van het tijdschrift	7
Vroegere onlinedatum	28-feb.-2024
DOI's	https://doi.org/10.1002/cbic.202400043
Status	Published - 2-apr.-2024

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10.1002/cbic.202400043Licentie: CC BY

Selective Aza‐Michael Addition to Dehydrated Amino Acids in Natural Antimicrobial PeptidesProof, 1,91 MBLicentie: 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.",

year = "2024",

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doi = "10.1002/cbic.202400043",

language = "English",

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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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