Copper(II) complex formation with a linear peptide encompassing the putative cell binding site of angiogenin(589 views) La Mendola D, Magrì A, Vagliasindi LI, Hansson Ö, Bonomo RP, Rizzarelli E
Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2010 Nov 28; 39(44): 10678-10684.
Istituto di Biostrutture e Bioimmagini-C.N.R.-Catania, Viale A. Doria 6, 95125, Catania, Italy.
Dipartimento di Scienze Chimiche, Università Degli Studi di Catania, Viale A. Doria 6, 95125, Catania, Italy
Consorzio Interuniversitario C.I.R.C.S.M.B., Via Celso Ulpiani 27, 70125, Bari, Italy
Department of Chemistry, University of Gothenburg, PO Box 462, SE-405 30 Gothenburg, Sweden
References: Not available.
Copper(II) complex formation with a linear peptide encompassing the putative cell binding site of angiogenin
Angiogenin is one of the more potent angiogenic factors known, whose activity may be affected by the presence of copper ions. Copper(II) complexes with the peptides encompassing the putative endothelial cell binding domain of angiogenin, Ac-KNGNPHREN-NH(2) and Ac-PHREN-NH(2), have been characterized by potentiometric, UV-vis, CD and EPR spectroscopic methods. The coordination features of all the copper complex species derived by both peptides are practically the same, as predictable because of the presence of a proline residue within their aminoacidic sequence. In particular, Ac-PHREN-NH(2) is really the aminoacidic sequence involved in the binding to copper(II). Thermodynamic and spectroscopic evidence are given that side chain oxygen donor atom of glutamyl residue is involved in the copper binding up to physiological pH. EPR parameters suggest that the carboxylate group is still involved also in the predominant species [Cu(L)H(-2)], the metal coordination environment being probably formed by N(Im), 2N(-), H(2)O in equatorial plane and an oxygen atom from COO(-) in apical position, or vice versa, with the carboxylate oxygen atom in the copper coordination plane and the water molecule confined to one of the apical positions. Moreover, the comparison with the thermodynamic and spectroscopic results in the case of the copper(ii) complex species formed by the single point mutated peptide, Ac-PHRQN-NH(2), provides further evidence of the presence of carboxylate oxygen atom in the copper coordination sphere.
Copper(II) complex formation with a linear peptide encompassing the putative cell binding site of angiogenin