Rapid Chemoselective Bioconjugation Through the Oxidative Coupling of Anilines and Aminophenols
| Autor: | Allie C. Obermeyer, Jacob M. Hooker, Christopher R. Behrens, Matthew B. Francis, Dante W. Romanini, Elan M. Katz |
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| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
chemistry.chemical_classification
Models Molecular Bioconjugation Aniline Compounds Molecular Structure Sodium periodate Stereochemistry General Chemistry Chromophore Aminophenols Crystallography X-Ray Biochemistry Combinatorial chemistry Small molecule Fluorescence Catalysis Article chemistry.chemical_compound Colloid and Surface Chemistry Capsid chemistry Thiol Oxidative coupling of methane Oxidation-Reduction Cysteine |
| Popis: | A highly efficient protein bioconjugation method is described involving the addition of anilines to o-aminophenols in the presence of sodium periodate. The reaction takes place in aqueous buffer at pH 6.5 and can reach high levels of completion in 2–5 min. The product of the reaction has been characterized using X-ray crystallography, which revealed that an unprecedented oxidative ring contraction occurs after the coupling step. The compatibility of the reaction with protein substrates has been demonstrated through the attachment of small molecules, polymer chains, and peptides to p-aminophenylalanine residues introduced into viral capsids through amber stop codon suppression. The coupling of anilines to o-aminophenol groups derived from tyrosine residues is also described. The compatibility of this method with thiol modification chemistry is shown through the attachment of a near-IR fluorescent chromophore to cysteine residues inside the viral capsid shells, followed by the attachment of integrin-targeting RGD peptides to anilines on the exterior surface. |
| Databáze: | OpenAIRE |
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