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

doi:10.1021/ic051577q

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

Chemistry

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

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 language	English
Pages (from-to)	472-474
Number of pages	3
Journal	Inorganic Chemistry
Volume	45
Issue number	2
DOIs	https://doi.org/10.1021/ic051577q
State	Published - Jan 23 2006

Funding

Funders	Funder number
National Institute of General Medical Sciences	F33GM072286

ASJC Scopus subject areas

Physical and Theoretical Chemistry
Inorganic Chemistry

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10.1021/ic051577q

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title = "De novo design and spectroscopic characterization of a dinucleating copper-binding pentadecapeptide",

abstract = "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 {\AA}.",

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doi = "10.1021/ic051577q",

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T1 - De novo design and spectroscopic characterization of a dinucleating copper-binding pentadecapeptide

AU - Rockcliffe, David A.

AU - Cammers, Arthur

AU - Murali, Ayaluru

AU - Russell, William K.

AU - DeRose, Victoria J.

PY - 2006/1/23

Y1 - 2006/1/23

N2 - 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.

AB - 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.

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

Abstract

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ASJC Scopus subject areas

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