Design of metal ion binding peptides
Copyright policy )Design of metal ion binding peptides
AbstractTwo 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. [A ZUHg]+ and [A ZUHg2]3+ having binding constants (Keq) of 3.106 and 2–104M−1, respectively. © 1994 John Wiley & Sons, Inc.
- University of Campania "Luigi Vanvitelli" Italy
- National Research Council Italy
- National Research Council Sri Lanka
- University Federico II of Naples Italy
Binding Sites, Molecular Sequence Data, Peptides, Cyclic, Kinetics, Azurin, Spectrophotometry, Drug Design, Metalloproteins, Amino Acid Sequence, Plastocyanin, Copper, Protein Binding
Binding Sites, Molecular Sequence Data, Peptides, Cyclic, Kinetics, Azurin, Spectrophotometry, Drug Design, Metalloproteins, Amino Acid Sequence, Plastocyanin, Copper, Protein Binding
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