Rapid sodium periodate cleavage of an unnatural amino acid enables unmasking of a highly reactive α-oxo aldehyde for protein bioconjugation

The α-oxo aldehyde is a highly reactive aldehyde for which many protein bioconjugation strategies exist. Here, we explore the genetic incorporation of a threonine-lysine dipeptide into proteins, harbouring a "masked" α-oxo aldehyde that is rapidly unveiled in four minutes. The reactive ald...

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Published inOrganic & biomolecular chemistry Vol. 18; no. 21; pp. 4 - 43
Main Authors Brabham, Robin L, Keenan, Tessa, Husken, Annika, Bilsborrow, Jacob, McBerney, Ryan, Kumar, Vajinder, Turnbull, W. Bruce, Fascione, Martin A
Format Journal Article
LanguageEnglish
Published CAMBRIDGE Royal Soc Chemistry 07.06.2020
Royal Society of Chemistry
Subjects
Aldehydes
Amino acids
Chemistry
Chemistry, Organic
Lysine
Physical Sciences
Proteins
Science & Technology
Threonine
CHEMISTRY
TRANSFER-RNA SYNTHETASE
PEPTIDE
LYSINE
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Summary:The α-oxo aldehyde is a highly reactive aldehyde for which many protein bioconjugation strategies exist. Here, we explore the genetic incorporation of a threonine-lysine dipeptide into proteins, harbouring a "masked" α-oxo aldehyde that is rapidly unveiled in four minutes. The reactive aldehyde could undergo site-specific protein modification by SPANC ligation. A genetically incorporated ThrK unnatural amino acid can undergo rapid periodate oxidation to reveal a reactive internal α-oxo aldehyde.
Bibliography:10.1039/d0ob00972e
Electronic supplementary information (ESI) available. See DOI
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ObjectType-Article-1
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ISSN:1477-0520
1477-0539
DOI:10.1039/d0ob00972e