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1.
Org Biomol Chem ; 18(30): 5982, 2020 Aug 05.
Article in English | MEDLINE | ID: mdl-32706355

ABSTRACT

Correction for 'Rapid sodium periodate cleavage of an unnatural amino acid enables unmasking of a highly reactive α-oxo aldehyde for protein bioconjugation' by Robin L. Brabham et al., Org. Biomol. Chem., 2020, 18, 4000-4003, DOI: 10.1039/D0OB00972E.

2.
Org Biomol Chem ; 18(21): 4000-4003, 2020 06 07.
Article in English | MEDLINE | ID: mdl-32427272

ABSTRACT

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.


Subject(s)
Aldehydes/metabolism , Amino Acids/metabolism , Periodic Acid/metabolism , Proteins/metabolism , Aldehydes/chemistry , Amino Acids/chemistry , Dipeptides/chemistry , Dipeptides/genetics , Dipeptides/metabolism , Molecular Conformation , Periodic Acid/chemistry , Proteins/chemistry , Proteins/genetics
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