Transition metal complexes of peptides. Models of the metal ion protein interactions.  Page description

Help  Print 
Back »
 

Details of project

  
Identifier
48352
Type K
Principal investigator Sóvágó, Imre
Title in Hungarian Az átmenetifémionok peptidekkel alkotott komplexei. A fémion-fehérje kölcsönhatás modellezése.
Title in English Transition metal complexes of peptides. Models of the metal ion protein interactions.
Panel Chemistry 1
Department or equivalent Department of Inorganic and Analytical Chemistry (University of Debrecen)
Participants Jószai, Viktória
Kállay, Csilla
Nagy, Eszter Márta
Nagy, Zoltán
Ősz, Katalin
Starting date 2005-01-01
Closing date 2008-12-31
Funding (in million HUF) 10.700
FTE (full time equivalent) 6.60
state closed project





 

Final report

  
Results in Hungarian
1. Multihisztidin peptidek réz(II)- és cink(II)komplexei: A hisztidin nitrogén donoratomok a peptidek elsődleges fémkötőhelyei. Ezek koordinációjával makrokelátok képződhetnek, amelyek stabilitása a hisztidinek számától és távolságától függ. A karboxilcsoportok jelenléte a cink(II)komplexek stabilitását növeli. A réz(II)ionok az amidcsoport deprotonálódását is indukálhatják, ami többmagvú komplexek képződéséhez vezet. A megkötött rézionok száma megegyezik a hisztidinek számával. 2. A prion protein peptid fragmenseinek fémkomplexei: Az oktarepeaten kívüli hisztidinek is stabilis rézkötőhelyek. A HuPrP(84-114) fragmensre kapott eredmények szerint a kötési helyek stabilitási sora: His111 > His96 >> His85. Egyéb átmenetifémek komplexeit is tanulmányoztuk, amelyek stabilitási sora a következő: Pd(II) > Cu(II) > Ni(II) > Zn(II) > Cd(II) ~ Co(II) > Mn(II). 3. Az amyloid-β peptid réz(II)komplexei: Az Aβ(1-16) peptidnek kiugróan nagy rézionaffinitása van. A terminális aminocsoport az elsődleges fémkötőhely, amit a hisztidinek koordinációja követ. Egy Aβ(1-16) molekula 4 réziont képes megkötni. Az egy- két- és három-magvú komplexeknek koordinációs izomerjei lehetnek, de a terminális aminocsoport és a szomszédos amidnitrogének koordinációja preferált.
Results in English
1. Copper(II) and zinc(II) complexes of multihistidine peptides: Histidyl residues are the primary metal binding sites resulting in the formation of macrochelates. The stabilities of macrochelates are influenced by the number and location of histidyl residues. The stability of zinc(II) complexes is enhanced by the presence of carboxylate functions. Formation of polynuclear complexes has also been detected and their nuclearities correspond to the number of histidyl sites. 2. Metal binding affinity of prion peptide fragments: Histidyl residues outside the octarerepat domain are effective copper binding sites. The results obtained for the copper(II) complexes of HuPrP(84-114) revealed the following stability order: His111 > His96 >> His85. Complex formation with several other transition elements has also been studied and their stability order: Pd(II) > Cu(II) > Ni(II) > Zn(II) > Cd(II) ~ Co(II) > Mn(II). 3. Copper(II) complexes of amyloid-β peptide fragments: Aβ(1-16) has an outstanding affinity towards the complexation with copper. The terminal amino group is the primary metal binding site, followed by the coordination of histidyl residues. One molecule of Aβ(1-16) can bind as much as four copper(II) ions. Various coordination isomers of the mono-, di- and tri-nuclear complexes can exist with a preference for the coordination via the terminal amino and subsequent amide groups.
Full text http://real.mtak.hu/1784/
Decision
Yes





 

List of publications

  
I. Sóvágó, K. Ősz, Z. Nagy, V. Rigó, D. Sanna, D. La Mendola, G. Di Natale, G. Pappalardo and E. Rizzarelli: Transition metal complexes of peptide fragments of prion protein, Advances in Coordination, Bioinorganic and Inorganic Chemistry, 2005
R.P. Bonomo, D. La Mendola, G. Pappalardo, E. Rizzarelli, I. Sóvágó: Coordination features of prion protein domains, Recent Developments in Bioinorganic Chemistry, Metal Complexes of Bioactive Molecules, 2006
K. Ősz, Z. Nagy, G. Pappalardo, G. Di Natale, D. Sanna, G. Micera, E. Rizzarelli and I. Sóvágó: Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain, Chemistry, European Journal, 13, 7129-7143, 2007
Cs. Kállay, I. Sóvágó, K. Várnagy: Nickel(II) complexes of oligopeptides containig aspartyl and glutamyl residues. Potentiometric and spectroscopic studies., Polyhedron, 26, 811-817, 2007
Cs. Kállay, Z. Nagy, K. Várnagy, G. Malandrinos, N. Hadjiliadis, I. Sóvágó: Thermodynamic and structural characterization of the copper(II) complexes of peptides containing both histidyl and aspartyl residues., Bioinorg. Chem. Appl., 2007
K. Zavitsanos, A.M. P.C. Nunes, G. Malandrinos, C. Kállay, I. Sóvágó, V. Magafa, P. Cordopatis, N. Hadjiliadis: Interaction of Cu(II) and Ni(II) with the 63-93 fragment of histone H2B., Dalton Transactions, 6179-6187, 2008
C. Damante, K. Ősz, Z. Nagy, G. Pappalardo, G. Grasso, G. Impellizzeri, E. Rizzarelli, I. Sóvágó: Metal ion interactions within the 1-16 N-terminal region of beta-amyloid, J. Peptide Science, 14, 87,, 2008
K. Ősz: A new, model-free calculation method to determine the coordination modes and distribution of copper(II) among the metal binding sites of multihistidine peptides using circular dichroism spectroscopy, J. Inorg. Biochem., 102, 2184-2195, 2008
I. Sóvágó, K. Ősz, Z. Nagy, G. Pappalardo, G. Di Natale, D. La Mendola, D. Sanna, E. Rizzarelli: Studies on the metal binding affinity of histidyl residues inside and outside the octarepeat domain of prion protein, 9th International Symposium on Applied Bioinorganic Chemistry, Naples, Italy, 2006
I. Sóvágó: Metal binding affinity and selectivity of peptides containing histidyl residues, 4th EuCheMS Conference on Nitrogen Ligands, Garmisch-Pertenkirchen, Germany, 2008
I. Sóvágó: Comparison of the metal binding affinities of prion and amyloid peptide fragments, Eurobic 9, Wroclaw, Poland, 2008
G. Di Natale, G. Grasso, G. Impellizzeri, D. La Mendola, G. Micera, N. Mihala, Z. Nagy, K. Ősz, G. Pappalardo, V. Rigó, E. Rizzarelli, D. Sanna and I. Sóvágó: Copper(II) interaction with unstructured prion domain outside the octarepat region, Inorganic Chemistry, 20, 7214-7225, 2005
Cs. Kállay, K. Várnagy, G. Malandrinos, N. Hadjiliadis, D. Sanna, I. Sóvágó: Copper(II) complexes of terminally protected pentapeptides containing three histidyl residues in alternating positions, Ac-His-Xaa-His-Yaa-His-NH2, Dalton Transactions, 4545-4552, 2006
D. Grasso, G. Grasso, V. Guantieri, G. Impellizzeri, C. La Rosa, D. Milardi, G. Micera, K. Ősz, G. Pappalardo, E. Rizzarelli, D. Sanna and I. Sóvágó: Environmental effects on a Prion's Helix II domain: Copper(II) and membrane interactions with PrP180-193 and its analogues., Chemistry European Journal, 12, 537-547, 2006
I. Sóvágó, K. Ősz: Metal Ion Selectivity of Oligopeptides, Dalton Transactions, 3841-3854, 2006
V. Jószai, Z. Nagy, K. Ősz, D. Sanna, G. Di Natale, D. La Mendola, G. Pappalardo, E. Rizzarelli, I. Sóvágó: Transition metal complexes of terminally protected peptides containing histidyl residues, Journal of Inorganic Biochemistry, 100, 1399-1409, 2006
C. Kállay, K. Ősz, A. Dávid, Z. Valastyán G. Malandrinos, N. Hadjiliadis, I. Sóvágó,: Zinc(II) binding ability of tri-, tetra- and pentapeptides containing two or three histidyl residues, Dalton Transactions, 4040-4047, 2007
C.A. Damante, K. Ősz, Z. Nagy, G. Pappalardo, G. Grasso, G. Impellizzeri, E. Rizzarelli, I. Sóvágó: The metal loading ability of beta-amyloid N-terminus: A combined potentiometric and spectroscopic study of copper(II) complexes with beta-amyloid(1-16). its short or mutated fragments and its polyethylene glycol (PEG)-ylated analogue., Inorg. Chem., 47, 9669-9683., 2008
G. Di Natale, C.A. Damante, Z. Nagy, K. Ősz, G. Pappalardo, E. Rizzarelli, I. Sóvágó,: Copper(II) binding to two novel histidine containing model hexapeptides: Evidence for a metal ion driven turn conformation., J. Inorg. Biochem., 102, 2012-2019, 2008
S. Rajkovic, C. Kállay, R. Serényi, G. Malandrinos, N. Hadjiliadis, D. Sanna, I. Sóvágó: Complex formation processes of terminally protected peptides containing two or three histidyl residues. Characterization of the mixed metal complexes of peptides., Dalton Transactions, 5059-5071, 2008
C. Kállay, K. Várnagy, G. Malandrinos, N. Hadjiliadis, D. Sanna, I. Sóvágó: Thermodynamic and structural characterization of the macrochelates formed in the reactions of copper(II) and zinc(II) ions with peptides of histidine, Inorg. Chim. Acta, 362, 935-945, 2009



Back »