Two cyclic and branched peptides (PLA and AZU) were synthesized with the aim of reproducing the active site of the blue copper proteins plastocyanin and azurin. Both peptides, designed on the basis of the x-ray structures of Poplar plastocyanin and Alcaligenes denitrificans azurin. contain the same coordinating residues of the parent native proteins. The visible spectra of PLA in the presence of equimolar amount of Cu(II) strongly support the interaction between the peptide and copper(II) ion. The CD titration of AZU with the Hg(II) ion indicates for the formation of two species.
Design of Metal Ion Binding Peptide / Fattorusso, R.; Morelli, G.; Lombardi, Angelina; Nastri, Flavia; Maglio, O.; D'Auria, Gabriella; Pedone, C.; Pavone, Vincenzo. - In: BIOPOLYMERS. - ISSN 0006-3525. - STAMPA. - 37:6(1995), pp. 401-410. [10.1002/bip.360370607]
Design of Metal Ion Binding Peptide
G. MORELLI;LOMBARDI, ANGELINA;NASTRI, FLAVIA;D'AURIA, GABRIELLA;PAVONE, VINCENZO
1995
Abstract
Two cyclic and branched peptides (PLA and AZU) were synthesized with the aim of reproducing the active site of the blue copper proteins plastocyanin and azurin. Both peptides, designed on the basis of the x-ray structures of Poplar plastocyanin and Alcaligenes denitrificans azurin. contain the same coordinating residues of the parent native proteins. The visible spectra of PLA in the presence of equimolar amount of Cu(II) strongly support the interaction between the peptide and copper(II) ion. The CD titration of AZU with the Hg(II) ion indicates for the formation of two species.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
