Luminol anchors improve the electrochemical-tyrosine-click labelling of proteins

Depienne, Sébastien; Álvarez-Dorta, Dimitri; Croyal, Mikaël; Temgoua, Ranil Clément Tonleu; Charlier, Cathy; Deniaud, David; Mével, Mathieu; Boujtita, Mohammed; Gouin, Sébastien G.

doi:10.1039/d1sc04809k

Cited by 19 publications

(12 citation statements)

References 52 publications

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“…We found that purging the buffer solution with Argon reduces this substantially. On the other hand use of the reported electrochemical oxidation method for TAD reagents 25,35 allows avoiding this side effect.…”

Section: Tad Modication Of Recombinant Proteinsmentioning

confidence: 99%

Triazolinedione protein modification: from an overlooked off-target effect to a tryptophan-based bioconjugation strategy

et al. 2022

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Section: Tad Modication Of Recombinant Proteinsmentioning

confidence: 99%

Triazolinedione protein modification: from an overlooked off-target effect to a tryptophan-based bioconjugation strategy

et al. 2022

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“…The use of N -methyl luminol and 1-methyl-4-phenylurazole derivatives as electrochemically active small-molecule modification reagents was investigated, with successful modification of a protected model octapeptide angiotensin II at the native tyrosine residue (Scheme B). Improved reaction efficiencies for both of the second-generation reagents ( N -methyl luminol and 1-methyl-4-phenylurazole) were achieved compared to the original phenylurazolean observation which was further corroborated by Gouin and co-workers in a 2021 study . However, Nakamura and co-workers observed significant dual modification of angiotensin II on the phenolic side chain of the tyrosine residue using N -methyl luminol.…”

Section: Indirect Electrochemical Approachesmentioning

confidence: 99%

Electrochemistry for the Chemoselective Modification of Peptides and Proteins

2021

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Although electrochemical strategies for small-molecule synthesis are flourishing, this technology has yet to be fully exploited for the mild and chemoselective modification of peptides and proteins. With the growing number of diverse peptide natural products being identified and the emergence of modified proteins as therapeutic and diagnostic agents, methods for electrochemical modification stand as alluring prospects for harnessing the reactivity of polypeptides to build molecular complexity. As a mild and inherently tunable reaction platform, electrochemistry is arguably well-suited to overcome the chemo- and regioselectivity issues which limit existing bioconjugation strategies. This Perspective will showcase recently developed electrochemical approaches to peptide and protein modification. The article also highlights the wealth of untapped opportunities for the production of homogeneously modified biomolecules, with an eye toward realizing the enormous potential of electrochemistry for chemoselective bioconjugation chemistry.

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“…However, this is only possible for very large proteins such as antibodies that generally is around 10–15 nm in size. MAUra is known to react with tyrosine under single electron transfer (SET) conditions, and as ruthenium photo‐catalyst catalyzes both SET and 1 O 2 generation, both Tyr and His can be labeled [56–58] …”

Section: Alkaline Amino Acid Residuesmentioning

confidence: 99%

“…MAUra is known to react with tyrosine under single electron transfer (SET) conditions, and as ruthenium photo-catalyst catalyzes both SET and 1 O 2 generation, both Tyr and His can be labeled. [56][57][58] In recent years, a new type of CÀ H functionalization for the selective reaction with His has emerged. The C2 position of the imidazole sidechain is electrophilic.…”

Section: Histidinementioning

confidence: 99%

Chemical Conjugation to Less Targeted Proteinogenic Amino Acids

2022

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Protein bioconjugates are in high demand for applications in biomedicine, diagnostics, chemical biology and bionanotechnology. Proteins are large and sensitive molecules containing multiple different functional groups and in particular nucleophilic groups. In bioconjugation reactions it can therefore be challenging to obtain a homogeneous product in high yield. Numerous strategies for protein conjugation have been developed, of which a vast majority target lysine, cysteine and to a lesser extend tyrosine. Likewise, several methods that involve recombinantly engineered protein tags have been reported. In recent years a number of methods have emerged for chemical bioconjugation to other amino acids and in this review, we present the progress in this area.

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Luminol anchors improve the electrochemical-tyrosine-click labelling of proteins

Abstract: We assessed the relative efficiencies of tyrosine anchors in the electrochemical conjugation of peptides and proteins. Luminol derivatives showed faster reaction kinetics, complete tyrosine-chemoselectivity, and possible double modification.

Cited by 19 publications

References 52 publications

Triazolinedione protein modification: from an overlooked off-target effect to a tryptophan-based bioconjugation strategy

Triazolinedione protein modification: from an overlooked off-target effect to a tryptophan-based bioconjugation strategy

Electrochemistry for the Chemoselective Modification of Peptides and Proteins

Chemical Conjugation to Less Targeted Proteinogenic Amino Acids

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