Vancomycin (Van) is a glycopeptide antibiotic active against Gram positive infections. Recently, it was found that several biological effects of Van are also related to its ability to bind both Cu(II) and Zn(II) metal ions under physiological/neutral conditions1. Its biological activity is due to a selective binding to D-Ala-D-Ala terminus of peptidoglycan precursor hampering the formation of the bacterial cell wall. Starting from these two different interaction modes of Van, i.e. by the direct interaction with [IrCp*Cl2]2 or by “trojan-horse” strategy exploiting the D-Ala-D-Ala anchoring system2 and alternative to the classical biotin/(strept)avidin3-4, we focused our attention on the possibility to obtain two different hybrid imine reductases, i.e. Metallo Peptides (M-Ps) and Artificial Metalloenzymes (Ar-Ms) to be used in the ATH of cyclic imines5.
New hybrid imine reductases based on Vancomycin for the asymmetric reduction of cyclic imines in aqueous buffer / G. Facchetti, I. Rimoldi. ((Intervento presentato al 34. convegno New Trends in Organic Synthesis tenutosi a Milano nel 2019.
New hybrid imine reductases based on Vancomycin for the asymmetric reduction of cyclic imines in aqueous buffer
G. Facchetti;I. Rimoldi
2019
Abstract
Vancomycin (Van) is a glycopeptide antibiotic active against Gram positive infections. Recently, it was found that several biological effects of Van are also related to its ability to bind both Cu(II) and Zn(II) metal ions under physiological/neutral conditions1. Its biological activity is due to a selective binding to D-Ala-D-Ala terminus of peptidoglycan precursor hampering the formation of the bacterial cell wall. Starting from these two different interaction modes of Van, i.e. by the direct interaction with [IrCp*Cl2]2 or by “trojan-horse” strategy exploiting the D-Ala-D-Ala anchoring system2 and alternative to the classical biotin/(strept)avidin3-4, we focused our attention on the possibility to obtain two different hybrid imine reductases, i.e. Metallo Peptides (M-Ps) and Artificial Metalloenzymes (Ar-Ms) to be used in the ATH of cyclic imines5.File | Dimensione | Formato | |
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