Palladium-unleashed proteins: gentle aldehyde decaging for site-selective protein modification

Robin Louis Brabham; Richard James Spears; Julia Walton; Swati Tyagi; Edward Lemke; Martin Anthony Fascione

Palladium-unleashed proteins: gentle aldehyde decaging for site-selective protein modification

Robin Louis Brabham, Richard James Spears, Julia Walton, Swati Tyagi, Edward Lemke, Martin Anthony Fascione

Chemistry

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

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 decade 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.

Original language	English
Pages (from-to)	1501-1504
Number of pages	4
Journal	Chemical Communications
Volume	54
Publication status	Published - 6 Feb 2018

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Palladium-unleashed proteins: gentle aldehyde decaging for site-selective protein modificationFinal published version, 2.3 MBLicence: CC BY

http://pubs.rsc.org/en/content/articlepdf/2018/CC/C7CC07740HLicence: Unspecified

Tandem organocatalysis for the bi-functional modification of proteins
FASCIONE, M. A. (Principal investigator)
EPSRC
1/11/17 → 31/10/18
Project: Research project (funded) › Research
Technologies for the Future
THOMAS-OATES, J. E. (Principal investigator) & JOHNSON, S. D. (Co-investigator)
EPSRC
1/04/15 → 31/03/16
Project: Research project (funded) › Research

Cite this

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title = "Palladium-unleashed proteins: gentle aldehyde decaging for site-selective protein modification",

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 decade 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.",

author = "Brabham, {Robin Louis} and Spears, {Richard James} and Julia Walton and Swati Tyagi and Edward Lemke and Fascione, {Martin Anthony}",

year = "2018",

month = feb,

day = "6",

language = "English",

volume = "54",

pages = "1501--1504",

journal = "Chemical Communications",

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T1 - Palladium-unleashed proteins: gentle aldehyde decaging for site-selective protein modification

AU - Brabham, Robin Louis

AU - Spears, Richard James

AU - Walton, Julia

AU - Tyagi, Swati

AU - Lemke, Edward

AU - Fascione, Martin Anthony

PY - 2018/2/6

Y1 - 2018/2/6

N2 - 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 decade 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.

AB - 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 decade 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.

M3 - Article

SN - 1359-7345

VL - 54

SP - 1501

EP - 1504

JO - Chemical Communications

JF - Chemical Communications

ER -

Palladium-unleashed proteins: gentle aldehyde decaging for site-selective protein modification

Abstract

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Projects

Tandem organocatalysis for the bi-functional modification of proteins

Technologies for the Future

Cite this