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 (R) C250L and coated with polyelectrolytes by the layer-by-layer method.
Botta, G., Delfino, M., Guazzaroni, M., Crestini, C., Onofri, S., Saladino, R. (2013). Selective synthesis of DOPA and DOPA peptides by native and immobilized tyrosinase in organic solvent. CHEMPLUSCHEM, 78, 325-330 [10.1002/cplu.201200300].
Selective synthesis of DOPA and DOPA peptides by native and immobilized tyrosinase in organic solvent
CRESTINI, CLAUDIA;
2013-01-01
Abstract
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 (R) C250L and coated with polyelectrolytes by the layer-by-layer method.| File | Dimensione | Formato | |
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