Keywords: Azurin, Binding Protein, Copper Ion, Cyclopeptide, Mercury, Metal Ion, Plastocyanin, Alcaligenes, Article, Binding Affinity, Circular Dichroism, Nonhuman, Peptide Synthesis, Protein Binding, Protein Structure, Ultraviolet Spectroscopy, X Ray Analysis, Amino Acid Sequence, Binding Sites, Drug Design, Kinetics, Metalloproteins, Molecular Sequence Data, Spectrophotometry, Achromobacter Denitrificans, Populus Berolinensis, Chemical Synthesis, Metabolism, Chemistry, Methods,
Affiliations: Department of Chemistry, Research Ctr. on Bioactive Peptides, University of Naples Federico II, via Mezzocannone 4, 80134 Napoli, Italy
References: Not available.
Design of metal ion binding peptides
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, [AZUHg]+ and [AZUHg2]3+ having binding constants (Keq) of 3.10(6) and 2.10(4) M-1, respectively.
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I * Copper(II) complexes of rat amylin fragments(517 views) Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721. Impact Factor:3.838 ViewExport to BibTeXExport to EndNote
Vitiello M, Finamore E, Falanga A, Raieta K, Cantisani M, Galdiero F, Pedone C, Galdiero M, Galdiero S * Fusion in Coq(578 views) Lecture Notes In Computer Science (ISSN: 0302-9743, 0302-974335404636319783540463634, 0302-974335402975459783540297543), 2001; 2178LNCS: 583-596. Impact Factor:0.415 ViewExport to BibTeXExport to EndNote