The effect of point mutations on copper(II) complexes with peptide fragments encompassing the 106-114 region of human prion protein (835 views)
Monatshefte Fur Chemie (ISSN: 0026-9247), 2011 Apr; 142(4): 411-419.
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Paper type: Journal Article,
Impact factor: 1.532, 5-year impact factor: 1.543
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79955842018&partnerID=40&md5=20c7d7c595df14b2a5dd0a029fc3ee76
Keywords: Bioinorganic Chemistry, Metal Complexes, Peptides, Prion Proteins,
Affiliations:
*** IBB - CNR ***
Department of Inorganic and Analytical Chemistry, University of Debrecen, Debrecen 4010, Hungary
Department of Colloid Chemistry, University of Debrecen, Debrecen 4010, Hungary
CNR Institute of Biomolecular Chemistry, Traversa La Crucca 3, Baldinca-Li Punti (Sassari) 07040, Italy
Department of Chemical Sciences, University of Catania, V.le A. Doria 6, Catania 95125, Italy
References:
Not available.
Monatshefte Fur Chemie (ISSN: 0026-9247), 2011 Apr; 142(4): 411-419.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.532, 5-year impact factor: 1.543
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79955842018&partnerID=40&md5=20c7d7c595df14b2a5dd0a029fc3ee76
Keywords: Bioinorganic Chemistry, Metal Complexes, Peptides, Prion Proteins,
Affiliations:
*** IBB - CNR ***
Department of Inorganic and Analytical Chemistry, University of Debrecen, Debrecen 4010, Hungary
Department of Colloid Chemistry, University of Debrecen, Debrecen 4010, Hungary
CNR Institute of Biomolecular Chemistry, Traversa La Crucca 3, Baldinca-Li Punti (Sassari) 07040, Italy
Department of Chemical Sciences, University of Catania, V.le A. Doria 6, Catania 95125, Italy
References:
Not available.
The effect of point mutations on copper(II) complexes with peptide fragments encompassing the 106-114 region of human prion protein
The tetrapeptides Ac-SKHM-NH(2), Ac-TKHM-NH(2), Ac-MKHS-NH(2), Ac-S(OMe)KHM-NH(2), and Ac-MKHS(OMe)-NH(2) and the nonapeptides Ac-KTNSKHMAG-NH(2) and Ac-KTNMKHSAG-NH(2) were synthesized and their copper(II) complexes were studied by potentiometric, UV-Vis, circular dichroism (CD), and electron paramagnetic resonance (EPR) spectroscopic methods. These peptides mimic the 109-112 and 106-114 residues of the sequence of human prion protein. The imidazole-N donor atoms of histidyl residues were found to be the primary metal binding sites of all peptide fragments. This binding mode provides a good possibility for the cooperative deprotonation and metal ion coordination of two amide functions preceding histidine. The (N(im),N(-),N(-))-bonded species predominate in the pH range 5.5-7.0 and the free coordination sites of these species make possible the metal binding of weakly coordinating side chains. The comparison of the potentiometric and spectroscopic results revealed the stabilizing role of the oxygen donors of seryl, threonyl, or methoxyseryl residues of Ac-SKHM-NH(2), Ac-TKHM-NH(2), Ac-S(OMe)KHM-NH(2), and Ac-KTNSKHMAG-NH(2) containing the mutations in position 109. These interactions were, however, not observed in the peptides containing the specific amino acids in other locations of the peptide sequence.
The tetrapeptides Ac-SKHM-NH(2), Ac-TKHM-NH(2), Ac-MKHS-NH(2), Ac-S(OMe)KHM-NH(2), and Ac-MKHS(OMe)-NH(2) and the nonapeptides Ac-KTNSKHMAG-NH(2) and Ac-KTNMKHSAG-NH(2) were synthesized and their copper(II) complexes were studied by potentiometric, UV-Vis, circular dichroism (CD), and electron paramagnetic resonance (EPR) spectroscopic methods. These peptides mimic the 109-112 and 106-114 residues of the sequence of human prion protein. The imidazole-N donor atoms of histidyl residues were found to be the primary metal binding sites of all peptide fragments. This binding mode provides a good possibility for the cooperative deprotonation and metal ion coordination of two amide functions preceding histidine. The (N(im),N(-),N(-))-bonded species predominate in the pH range 5.5-7.0 and the free coordination sites of these species make possible the metal binding of weakly coordinating side chains. The comparison of the potentiometric and spectroscopic results revealed the stabilizing role of the oxygen donors of seryl, threonyl, or methoxyseryl residues of Ac-SKHM-NH(2), Ac-TKHM-NH(2), Ac-S(OMe)KHM-NH(2), and Ac-KTNSKHMAG-NH(2) containing the mutations in position 109. These interactions were, however, not observed in the peptides containing the specific amino acids in other locations of the peptide sequence.
The effect of point mutations on copper(II) complexes with peptide fragments encompassing the 106-114 region of human prion protein
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The effect of point mutations on copper(II) complexes with peptide fragments encompassing the 106-114 region of human prion protein
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Impact Factor: 3.647
View Export to BibTeX Export to EndNote
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Impact Factor: 5.476
View Export to BibTeX Export to EndNote
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Impact Factor: 2.028
View Export to BibTeX Export to EndNote
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Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2010; 39(30): 7046-7053.
Impact Factor: 3.647
View Export to BibTeX Export to EndNote
Bellia F, La Mendola D, Pedone C, Rizzarelli E, Saviano M, Vecchio G
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Chem Soc Rev (ISSN: 1460-4744, 0306-0012, 1460-4744electronic), 2009 Sep; 38(9): 2756-2781.
Impact Factor: 20.086
View Export to BibTeX Export to EndNote
La Mendola D, Pietropaolo A, Pappalardo G, Zannoni C, Rizzarelli E
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Current Alzheimer Research (ISSN: 1567-2050), 2009 Jun; 6(3): N/D-N/D.
Impact Factor: 4.971
View Export to BibTeX Export to EndNote
La Mendola D, Pietropaolo A, Pappalardo G, Zannoni C, Rizzarelli E
* Prion proteins leading to neurodegeneration (541 views)
Current Alzheimer Research (ISSN: 1567-2050), 2008 Dec; 5(6): 579-590.
Impact Factor: 4.132
View Export to BibTeX Export to EndNote
Di Natale G, Damante CA, Nagy Z, Osz K, Pappalardo G, Rizzarelli E, Sóvágó I
* Copper(II) binding to two novel histidine-containing model hexapeptides: evidence for a metal ion driven turn conformation (545 views)
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Impact Factor: 3.133
View Export to BibTeX Export to EndNote
Joszal V, Nagy Z, Osz K, Sanna D, Di Natale G, La Mendola D, Pappalardo G, Rizzarelli E, Sovago I
* Transition metal complexes of terminally protected peptides containing histidyl residues (678 views)
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Impact Factor: 2.654
View Export to BibTeX Export to EndNote
Di Natale G, Impellizzeri G, Pappalardo G
* Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study (531 views)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2005 Feb 7; 3(3): 490-497.
Impact Factor: 2.547
View Export to BibTeX Export to EndNote
Bonomo RP, Cucinotta V, Giuffrida A, Impellizzeri G, Magrì A, Pappalardo G, Rizzarelli E, Santoro AM, Tabbì G, Vagliasindi LI
* A re-investigation of copper coordination in the octa-repeats region of the prion protein (464 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2005 Jan 7; (1): 150-158.
Impact Factor: 3.003
View Export to BibTeX Export to EndNote
Tizzano B, Marasco D, Benedetti E, De Capua A, Palladino P, Pedone C, Perretta G, Rossi F, Ragone R, Ruvo M
* Conformational conversion of prion proteins: Role synthetic PRP 173-195 fibrillogenic peptide (446 views)
Peptide Revolution, 2004; N/D: N/D-N/D.
Impact Factor: 4.659
View Export to BibTeX Export to EndNote
Pappalardo G, Impellizzeri G, Campagna T
* Copper(II) binding of prion protein's octarepeat model peptides (668 views)
Inorg Chim Acta (ISSN: 0020-1693), 2004; 357(1): 185-194.
Impact Factor: 1.554
View Export to BibTeX Export to EndNote
23 Records (21 excluding Abstracts).
Total impact factor: 130.686 (121.056 excluding Abstracts).
Total 5 year impact factor: 129.652 (120.185 excluding Abstracts).
Total impact factor: 130.686 (121.056 excluding Abstracts).
Total 5 year impact factor: 129.652 (120.185 excluding Abstracts).
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