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Your search keyword '"Brabham RL"' showing total 2 results
Start Over Author "Brabham RL" Topic aldehydes
2 results on '"Brabham RL"'

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

Author

Brabham RL, Keenan T, Husken A, Bilsborrow J, McBerney R, Kumar V, Turnbull WB, and Fascione MA

Subjects
Aldehydes chemistry, Amino Acids chemistry, Dipeptides chemistry, Dipeptides genetics, Dipeptides metabolism, Molecular Conformation, Periodic Acid chemistry, Proteins chemistry, Proteins genetics, Aldehydes metabolism, Amino Acids metabolism, Periodic Acid metabolism, Proteins metabolism
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.

Published
2020
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2. Palladium-unleashed proteins: gentle aldehyde decaging for site-selective protein modification.

Author

Brabham RL, Spears RJ, Walton J, Tyagi S, Lemke EA, and Fascione MA

Subjects
Molecular Structure, Aldehydes metabolism, Organometallic Compounds chemistry, Palladium chemistry, Proteins chemistry, Proteins metabolism
Abstract

Protein bioconjugation frequently makes use of aldehydes as reactive handles, with methods for their installation being highly valued. Here a new, powerful strategy to unmask a reactive protein aldehyde is presented. A genetically encoded caged glyoxyl aldehyde, situated in solvent-accessible locations, can be rapidly decaged through treatment with just one equivalent of allylpalladium(ii) chloride dimer at physiological pH. The protein aldehyde can undergo subsequent oxime ligation for site-selective protein modification. Quick yet mild conditions, orthogonality and powerful exposed reactivity make this strategy of great potential in protein modification.

Published
2018
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