De novo design and spectroscopic characterization of a dinucleating copper-binding pentadecapeptide

David A. Rockcliffe, Arthur Cammers, Ayaluru Murali, William K. Russell, Victoria J. DeRose

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


A spectroscopic study of aqueous solutions of Ac-WGHGHGHGPGHGHGH-NH 2 (HGP) indicates that copper(II) binds to the peptide to form a 2:1 Cu2+/HGP complex with four nitrogen atoms in the copper coordination environment. Electron paramagnetic resonance (EPR) and UV-visible data suggest copper binding through the peptide backbone and imidazole nitrogen donors. Circular dichroism data show that HGP is unbound below pH 5.5 and is copper-saturated at pH 9 and above. The apo form of the peptide is unstructured in solution and is organized into a turn conformation in the presence of 2 mol equiv of Cu2+ at basic pH. EPR measurements for 2:1 Cu 2+/HGP solutions in the g = 2 region and within the pH range 7-11 exhibit axial spectra. A molecular-mechanics-minimized model of the Cu 2+/HGP complex gave a Cu⋯Cu separation of 8 Å.

Original languageEnglish (US)
Pages (from-to)472-474
Number of pages3
JournalInorganic Chemistry
Issue number2
StatePublished - Jan 23 2006
Externally publishedYes

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry


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