We present a DFT study of the structural and spectroscopic properties of the complex formed by Cu2? with the peptide fragment Ac-PHREN-NH2, which encompasses the putative cell binding domain of angiogenin, as well as with its Ac-PHRQN-NH2 variant. Analysis of structures, energies and spectroscopic parameters has allowed to conclude that the metal coordination environment at pH 8 is formed by a nitrogen atom of His, two deprotonated amide groups, and an oxygen atom from the COO- side chain of Glu, in nice agreement with recent experimental results (La Mendola et al. in Dalton Trans, 39:10678, 2010). Moreover, DFT results allowed to reveal that the Glu side chain of the Ac-PHREN-NH2 peptide is coordinated in equatorial position, in a tetrahedrically distorted square planar arrangement, fully disclosing the effects of Cu2? binding on the structural properties of this key angiogenin portion. In the Ac-PHRQN-NH2 variant, the carboxylate group is replaced by a H2O molecule in a coordination arrangement similar to that of the wild-type system.

Bertini, L., Bruschi, M., Romaniello, M., Zampella, G., Tiberti, M., Barbieri, V., et al. (2012). Copper coordination to the putative cell binding site of angiogenin: a DFT investigation. THEORETICAL CHEMISTRY ACCOUNTS, 131(3), 1-15 [10.1007/s00214-012-1186-y].

Copper coordination to the putative cell binding site of angiogenin: a DFT investigation

BERTINI, LUCA;BRUSCHI, MAURIZIO;ZAMPELLA, GIUSEPPE;TIBERTI, MATTEO;BARBIERI, VALENTINA;GRECO, CLAUDIO;FANTUCCI, PIERCARLO;DE GIOIA, LUCA
2012

Abstract

We present a DFT study of the structural and spectroscopic properties of the complex formed by Cu2? with the peptide fragment Ac-PHREN-NH2, which encompasses the putative cell binding domain of angiogenin, as well as with its Ac-PHRQN-NH2 variant. Analysis of structures, energies and spectroscopic parameters has allowed to conclude that the metal coordination environment at pH 8 is formed by a nitrogen atom of His, two deprotonated amide groups, and an oxygen atom from the COO- side chain of Glu, in nice agreement with recent experimental results (La Mendola et al. in Dalton Trans, 39:10678, 2010). Moreover, DFT results allowed to reveal that the Glu side chain of the Ac-PHREN-NH2 peptide is coordinated in equatorial position, in a tetrahedrically distorted square planar arrangement, fully disclosing the effects of Cu2? binding on the structural properties of this key angiogenin portion. In the Ac-PHRQN-NH2 variant, the carboxylate group is replaced by a H2O molecule in a coordination arrangement similar to that of the wild-type system.
Articolo in rivista - Articolo scientifico
Copper; Angiogenin; Density Fuctional Theory;
English
2012
131
3
1
15
1186
none
Bertini, L., Bruschi, M., Romaniello, M., Zampella, G., Tiberti, M., Barbieri, V., et al. (2012). Copper coordination to the putative cell binding site of angiogenin: a DFT investigation. THEORETICAL CHEMISTRY ACCOUNTS, 131(3), 1-15 [10.1007/s00214-012-1186-y].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/29957
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