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Design of metal ion binding peptides
Author(s) -
Fattorusso R.,
Morelli G.,
Lombardi A.,
Nastri F.,
Maglio O.,
D'Auria G.,
Pedone C.,
Pavone V.
Publication year - 1995
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360370607
Subject(s) - plastocyanin , chemistry , azurin , copper , copper protein , metal ions in aqueous solution , metal , titration , peptide , ion , stereochemistry , crystallography , inorganic chemistry , organic chemistry , biochemistry , photosystem i , chloroplast , gene
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. [A ZUHg] + and [A ZUHg 2 ] 3+ having binding constants (K eq ) of 3.10 6 and 2–10 4 M −1 , respectively. © 1994 John Wiley & Sons, Inc.