Selective Synthesis of DOPA and DOPA Peptides by Native and Immobilized Tyrosinase in Organic Solvent

3,4‐Dihydroxyphenylalanine (DOPA)‐containing peptides and proteins provide attractive design paradigms for pharmaceutical applications and engineering of synthetic polymers. An efficient and selective route to DOPA peptides by oxidation of L‐tyrosine derivatives with tyrosinase is reported. The effi...

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Bibliographic Details
Published in:ChemPlusChem (Weinheim, Germany) Germany), 2013-04, Vol.78 (4), p.325-330
Main Authors: Botta, Giorgia, Delfino, Michela, Guazzaroni, Melissa, Crestini, Claudia, Onofri, Silvano, Saladino, Raffaele
Format: Article
Language:English
Subjects:
biocatalysis
DOPA peptides
enzymes
immobilization
synthetic methods
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Summary:3,4‐Dihydroxyphenylalanine (DOPA)‐containing peptides and proteins provide attractive design paradigms for pharmaceutical applications and engineering of synthetic polymers. An efficient and selective route to DOPA peptides by oxidation of L‐tyrosine derivatives with tyrosinase is reported. The efficiency of the procedure was tested by using successively recycled tyrosinase immobilized on Eupergit®C250L and coated with polyelectrolytes by the layer‐by‐layer method. A direct route: Bioactive catechol derivatives, such as Boc‐Gly‐DOPA‐OMe (Boc=tert‐butoxycarbonyl, DOPA=3,4‐dihydroxyphenylalanine), have been synthesized from the corresponding L‐tyrosine (Tyr) derivatives (see scheme). The oxidation is performed with immobilized tyrosinase, from Agaricus bisporus, in CH2Cl2/buffer at room temperature under an O2 atmosphere.
ISSN:2192-6506
2192-6506
DOI:10.1002/cplu.201200300