Oxime Ligation: A Chemoselective Click‐Type Reaction for Accessing Multifunctional Biomolecular Constructs

Ulrich, Sébastien; Boturyn, Didier; Marra, Alberto; Renaudet, Olivier; Dumy, Pascal

doi:10.1002/chem.201302426

Cited by 224 publications

(210 citation statements)

References 147 publications

(86 reference statements)

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“…Genetic incorporation of a NNAA has proven to be an invaluable tool to address this problem. An anti-Her2 or anti-CXCR4 mAb containing site-specifically incorporated ACF was subjected to a bioorthogonal oxime ligation with a monomethyl auristatin F derivative, resulting in a highly homogeneous, stoichiometrycontrolled and stable ADC with excellent pharmacological properties ( Figure 3B) Kularatne et al, 2014;Ulrich et al, 2014). Similarly, instead of a chemical drug, the protein toxin saporin was conjugated to an anti-Her2 mAb through a heterobifunctional linker to generate immunotoxin ( Figure 3B) (Hutchins et al, 2012).…”

Section: Targeted Drug Deliverymentioning

confidence: 99%

Bioconjugation of therapeutic proteins and enzymes using the expanded set of genetically encoded amino acids

Lim

Kwon

2015

Critical Reviews in Biotechnology

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The last decade has witnessed striking progress in the development of bioorthogonal reactions that are strictly directed towards intended sites in biomolecules while avoiding interference by a number of physical and chemical factors in biological environment. Efforts to exploit bioorthogonal reactions in protein conjugation have led to the evolution of protein translational machineries and the expansion of genetic codes that systematically incorporate a range of non-natural amino acids containing bioorthogonal groups into recombinant proteins in a site-specific manner. Chemoselective conjugation of proteins has begun to find valuable applications to previously inaccessible problems. In this review, we describe bioorthogonal reactions useful for protein conjugation, and biosynthetic methods that produce proteins amenable to those reactions through an expanded genetic code. We then provide key examples in which novel protein conjugates, generated by the genetic incorporation of a non-natural amino acid and the chemoselective reactions, address unmet needs in protein therapeutics and enzyme engineering.

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Section: Targeted Drug Deliverymentioning

confidence: 99%

Bioconjugation of therapeutic proteins and enzymes using the expanded set of genetically encoded amino acids

Lim

Kwon

2015

Critical Reviews in Biotechnology

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“…Oxime click chemistry, the formation of an oxime bond by reaction between an aminooxy group and an aldehyde or ketone, has emerged as a robust strategy in areas such as bioconjugation [165]. Compared with primary amines, reactivity of hydroxylamine or alkoxylamine (aminooxy) groups towards carbonyls is significantly higher [166] and the formed oximes are much more stable against hydrolysis than corresponding imines [167].…”

Section: Oxime Click Chemistrymentioning

confidence: 99%

“Click” reactions in polysaccharide modification

Meng

Edgar

2016

Progress in Polymer Science

182

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Polysaccharide chemistry is enjoying accelerating development thanks to advances in synthetic techniques, biochemistry and solvents, which enable polysaccharide materials to be useful in a variety of demanding applications. Among the synthetic advances, click chemistry has reconfigured the realm of polysaccharide modification that previously was dominated by conventional synthetic approaches such as esterification and etherification. "Click" reactions provide mild, modular, and efficient modification pathways, and equally importantly allow us to synthesize derivatives with novel functionality, architecture, and properties, that are otherwise difficult to obtain via conventional methods. Herein, we review application in polysaccharide modification of six groups of click reactions; CuAAC (copper catalyzed alkyne/azide cycloaddition), metal-free [3+2] cycloaddition, Diels-Alder reaction, oxime click, thiol-Michael reaction, and thiol-ene reaction, as well as one click-like reaction that is the subject of our own research, olefin cross-metathesis.

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“…[13] We synthesized b-glucuronide-linked and aminooxylated MMAF (LBG-MMAF) for the production of RDCs through ac hemoselective oxime reaction. MMAF,amicrotubuledisrupting agent, has been widely exploited as ap romising payload owing to its extremely high potency.…”

Section: Angewandte Chemiementioning

confidence: 99%

Enzymatic Prenylation and Oxime Ligation for the Synthesis of Stable and Homogeneous Protein–Drug Conjugates for Targeted Therapy

Lee

Choi²,

Yun

et al. 2015

Angew Chem Int Ed

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Targeted therapy based on protein-drug conjugates has attracted significant attention owing to its high efficacy and low side effects. However, efficient and stable drug conjugation to a protein binder remains a challenge. Herein, a chemoenzymatic method to generate highly stable and homogenous drug conjugates with high efficiency is presented. The approach comprises the insertion of the CaaX sequence at the C-terminal end of the protein binder, prenylation using farnesyltransferase, and drug conjugation through an oxime ligation reaction. MMAF and an EGFR-specific repebody are used as the antitumor agent and protein binder, respectively. The method enables the precisely controlled synthesis of repebody-drug conjugates with high yield and homogeneity. The utility of this approach is illustrated by the notable stability of the repebody-drug conjugates in human plasma, negligible off-target effects, and a remarkable antitumor activity in vivo. The present method can be widely used for generating highly homogeneous and stable PDCs for targeted therapy.

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Oxime Ligation: A Chemoselective Click‐Type Reaction for Accessing Multifunctional Biomolecular Constructs

Cited by 224 publications

References 147 publications

Bioconjugation of therapeutic proteins and enzymes using the expanded set of genetically encoded amino acids

Bioconjugation of therapeutic proteins and enzymes using the expanded set of genetically encoded amino acids

“Click” reactions in polysaccharide modification

Enzymatic Prenylation and Oxime Ligation for the Synthesis of Stable and Homogeneous Protein–Drug Conjugates for Targeted Therapy

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