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A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein (360 visite)

La Mendola D, Magrì A, Campagna T, Campitiello MA, Raiola L, Isernia C, Hansson O, Bonomo RP, Rizzarelli E

Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2010 Jun 1; 16(21): 6212-6223.

Tipo di articolo: Journal Article, Research Support, Non-U. S. Gov'T, , Impact factor: 5.476, Impact factor a 5 anni: 5.477, Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77952728882&partnerID=40&md5=bfa042f2e7a6f2bdbe61b2849a22f99d

Parole chiave: Copper, Doppel Proteins, Helical Structures, Peptides, Prions, Amino Acid Residues, Aqueous Solutions, Asparagine Residue, Aspartates, Carboxylate Groups, Cd Measurements, Cd Spectra, Coordination Environment, Copper Complexes, Copper Ions, Epr Parameters, Helical Conformation, Helix Peptide, Histidine Residues, Loop Regions, Metal Binding, Metal-Binding Sites, N-Terminal Domains, Neurotoxicity, Peptide Conformation, Peptide Fragments, Physiological Ph Range, Potentiometric Titrations, Prion Protein, Protein Domains, Protein Functions, Secondary Structures, Spectroscopic Measurements, Spectroscopic Parameters, Spectroscopic Studies, Stability Constants, Transgenic Mice, Uv Region, Binding Energy, Biochemistry, Carboxylation, Complexation, Coordination Reactions, Data Storage Equipment, Electron Spin Resonance Spectroscopy, Metal Complexes, Metal Ions, Organic Acids, Ph Effects, Phosphatases, Plants (botany), Spectroscopic Analysis, Synthesis (chemical), Copper Compounds, Glycosylphosphatidylinositol Anchored Protein, Prnd Protein, Human, Amino Acid Sequence, Article, Circular Dichroism, Protein Binding, Protein Secondary Structure, Thermodynamics, Ultraviolet Spectrophotometry, Gpi-Linked Proteins, Protein Structure,

Affiliazioni: *** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università Degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy
Istituto di Biostrutlure e Bioimmagini, CNR, c/o Dipartimento di Scienze Chimiche Viale A. Doria 6, 95125 Catania, Italy
Department of Chemistry, University of Gothenburg, PO Box 462, SE-405 30 Gothenburg, Sweden
Istituto Nazionale di Biostrutture e Biosistemi, Consorzio Interuniversitario, Viale Medaglie d'oro 305, 00136 Roma, Italy
Département de Biochimie, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, QC, H3C 3J7, Canada
D partement de Biochimie, Universit de Montr al, C. P. 6128 Succursale Centre-Ville, Montr al, QC, H3C 3J7, Canada


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The doppel protein (Dpi) is the first homologue of the prion protein (PrP C) to be discovered; it is overexpressed in transgenic mice that lack the prion gene, resulting in neurotoxicity. The whole prion protein is able to inhibit Dpi neurotoxicity, and its N-terminal domain is the determinant part of the protein function. This region represents the main copper(II) binding site of PrP C. Dpi is able to bind at least one copper ion, and the specific metalbinding site has been identified as the histidine residue at the beginning of the third helical region. However, a reliable characterization of copper(II) coordination features has not been reported. In a previous paper, we studied the copper(II) interaction with a peptide that encompasses only the loop region potentially involved in metal binding. Nevertheless, we did not find a complete match between the EPR spectroscopic parameters of the copper(II) complexes formed with the synthesized peptide and those reported for the copper(II) binding sites of the whole protein. Herein, the synthesis of the human Dpi peptide fragment hDpl(122-139) (Ac-KPDNKLHQQVLWRLVQEL-NH 2) and its copper(II) complex species are reported. This peptide encompasses the third a helix and part of the loop linking the second and the third helix of human doppel protein. The single-point-mutated peptide, hDpl(122-139)D124N, in which aspartate 124 replaces an asparagine residue, was also synthesized. This peptide was used to highlight the role of the carboxylate group on both the conformation preference of the Dpi fragment and its copper(II) coordination features. NMR spectroscopic measurements show that the hDpl( 122-139) peptide fragment is in the prevailing ahelix conformation. It is localized within the 127-137 amino acid residue region that represents a reliable conformational mimic of the related protein domain. A comparison with the singlepoint-mutated hDpl(122-139)D124N reveals the significant role played by the aspartic residue in addressing the peptide conformation towards a helical structure. It is further confirmed by CD measurements. Potentiometric titrations were carried out in aqueous solutions to obtain the stability constant values of the species formed by copper(II) with the hDpl peptides. Spectroscopic studies (EPR, NMR, CD, UV/Vis) were performed to characterize the coordination environments of the different metal complexes. The EPR parameters of the copper(II) complexes with hDpl( 122-139) match those of the previously reported copper(II) binding sites of the whole hDpl. Addition of the copper(II) ion to the peptide fragment does not alter the helical conformation of hDpl(122-139), as shown by CD spectra in the far-UV region. The aspartate-driven preorganized secondary structure is not significantly modified by the involvement of Aspl24 in the copper(II) complex species that form in the physiological pH range. To elaborate on the potential role of copper(II) in the recently reported interaction between the PrP C and Dpi, the affinity of the copper(II) complexes towards the prion N terminus domain and the binding site of Dpi was reported. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.

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12 Records (9 escludendo Abstract e Conferenze).
Impact factor totale: 34.75 (26.371 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 34.954 (27.132 escludendo Abstract e Conferenze).







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