Copper(II), nickel(II) and zinc(II) complexes of N-acetyl-His-Pro-His-His-NH2: Equilibria, solution structure and enzyme mimicking

Jakab, Noémi; Jancsó, Attila; Gajda, Tamás; Gyurcsik, Béla; Rockenbauer, Antal

doi:10.1016/j.jinorgbio.2008.01.006

Cited by 35 publications

(27 citation statements)

References 52 publications

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“…The stability constants of CuHL and CuL species, being dominant below pH 7, calculated for the Cu + H x L = CuH x L equilibria (x = 1 and 0) are logK = 5.71 and 6.93. These data fit well to the values published for the {2N im } and {3N im } coordinated species of some other Pro-containing multihistidine peptides [41,42]. This coordination environment around the metal ion is also supported by the spectroscopic data of these complexes (k dÀd max = 690 (650) nm, g || = 2.322 (2.280), A || = 156 (163) G for CuHL (CuL), respectively).…”

Section: Interaction Of Ac-hhphg-nh 2 and Ac-hhphghhphg-nh 2 With Copsupporting

confidence: 87%

“…The determined pK values (see Table 1) representing the deprotonation processes are macroscopic constants and cannot be assigned to individual histidine residues. The pK values are very similar to those measured for other terminally protected short Hisrich peptides [41,42,[48][49][50][51][52], which reflect no specific interaction between the deprotonating groups of the ligands.…”

Section: Protonation Equilibria Of the Ligandssupporting

confidence: 74%

“…Our approach to explore the metal-binding features of HRG was to study systematically the metal-binding ability of oligopeptide fragments, as models, derived from the repeat-region of the His-Pro-rich domain of HRG and to investigate the effect of the increasing number of repeated pentapeptide segments on the stability and structure of the complexes formed. In a close relation to our previous works with histidine-rich [39,40] and histidine-proline-rich peptides [41,42], here we present an equilibrium and solution structural study on the interaction of the pentapeptide Ac-HHPHG-NH 2 (HP1) and its dimer Ac-HHPHGHHPHG-NH 2 (HP2) with zinc(II) and copper(II) ions (for the structures of the ligands, see Scheme 1).…”

Section: Introductionmentioning

confidence: 69%

“…The stability constant of ZnL (logK = 4.16, see Table 2) is considerably higher than that of the {2 N im } coordinated complex of Ac-HHVGD-NH 2 [48] or Ac-HPHOEt [49], suggesting the coordination of all the three imidazole rings. Above logK is approximately one logarithmic unit smaller compared to the parent zinc(II) complexes of the Ac-HPHPH-NH 2 and Ac-HHGH-NHMe peptides [42,48], but similar to that of the ZnL species of Ac-HPHH-NH 2 [41]. It seems likely that the presence of a proline residue in such short peptides results in a strained structure and thus lowers the stability of the {3N im } coordinated species when two histidines are in adjacent positions.…”

Section: Interaction Of Ac-hhphg-nh 2 and Ac-hhphghhphg-nh 2 With Zinmentioning

confidence: 93%

“…These results are discussed below, together with those of HP2. Titrations could be performed only up to pH $ 7.1 since above this pH precipitation occurred in parallel with the deprotonation process leading to ZnH -1 L, similarly to several other systems of N-terminally protected oligopeptides and zinc(II) [39,41,42,[48][49][50].…”

Section: Interaction Of Ac-hhphg-nh 2 and Ac-hhphghhphg-nh 2 With Zinmentioning

confidence: 99%

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Probing the Cu2+ and Zn2+ binding affinity of histidine-rich glycoprotein

Jancsó

Kolozsi

Gyurcsik

et al. 2009

Journal of Inorganic Biochemistry

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Section: Interaction Of Ac-hhphg-nh 2 and Ac-hhphghhphg-nh 2 With Copsupporting

confidence: 87%

Section: Protonation Equilibria Of the Ligandssupporting

confidence: 74%

Section: Introductionmentioning

confidence: 69%

Section: Interaction Of Ac-hhphg-nh 2 and Ac-hhphghhphg-nh 2 With Zinmentioning

confidence: 93%

Section: Interaction Of Ac-hhphg-nh 2 and Ac-hhphghhphg-nh 2 With Zinmentioning

confidence: 99%

See 3 more Smart Citations

Probing the Cu2+ and Zn2+ binding affinity of histidine-rich glycoprotein

Jancsó

Kolozsi

Gyurcsik

et al. 2009

Journal of Inorganic Biochemistry

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Harnessing the Flexibility of Peptidic Scaffolds to Control their Copper(II)‐Coordination Properties: A Potentiometric and Spectroscopic Study

Fragoso

Lamosa

Delgado

et al. 2013

Chemistry A European J

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Designing small peptides that are capable of binding Cu(2+) ions mainly through the side-chain functionalities is a hard task because the amide nitrogen atoms strongly compete for Cu(2+) ion coordination. However, the design of such peptides is important for obtaining biomimetic small systems of metalloenyzmes as well as for the development of artificial systems. With this in mind, a cyclic decapeptide, C-Asp, which contained three His residues and one Asp residue, and its linear derivative, O-Asp, were synthesized. The C-Asp peptide has two Pro-Gly β-turn-inducer units and, as a result of cyclization, and as shown by CD spectroscopy, its backbone is constrained into a more defined conformation than O-Asp, which is linear and contains a single Pro-Gly unit. A detailed potentiometric, mass spectrometric, and spectroscopic study (UV/Vis, CD, and EPR spectroscopy) showed that at a 1:1 Cu(2+)/peptide ratio, both peptides formed a major [CuHL](2+) species in the pH range 5.0-7.5 (C-Asp) and 5.5-7.0 (O-Asp). The corrected stability constants of the protonated species (log K*(CuH(O-Asp))=9.28 and log K*(CuH(C-Asp))=10.79) indicate that the cyclic peptide binds Cu(2+) ions with higher affinity. In addition, the calculated value of K(eff) shows that this higher affinity for Cu(2+) ions prevails at all pH values, not only for a 1:1 ratio but even for a 2:1 ratio. The spectroscopic data of both [CuHL](2+) species are consistent with the exclusive coordination of Cu(2+) ions by the side-chain functionalities of the three His residues and the Asp residue in a square-planar or square-pyramidal geometry. Nonetheless, although these data show that, upon metal coordination, both peptides adopt a similar fold, the larger conformational constraints that are present in the cyclic scaffold results in different behaviour for both [CuHL](2+) species. CD and NMR analysis revealed the formation of a more rigid structure and a slower Cu(2+)-exchange rate for [CuH(C-Asp)](2+) compared to [CuH(O-Asp](2+). This detailed comparative study shows that cyclization has a remarkable effect on the Cu(2+)-coordination properties of the C-Asp peptide, which binds Cu(2+) ions with higher affinity at all pH values, stabilizes the [CuHL](2+) species in a wider pH range, and has a slower Cu(2+)-exchange rate compared to O-Asp.

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Effect of the Peptidic Scaffold in Copper(II) Coordination and the Redox Properties of Short Histidine‐Containing Peptides

Fragoso

Carvalho

Rousselot‐Pailley

et al. 2015

Chemistry A European J

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A linear decapeptide containing three His and one Asp residues and a β-turn-inducing dProPro unit was synthesised. A detailed potentiometric, mass spectrometric and spectroscopic study showed that at a 1:1 ratio of CCu /Cpeptide this peptide formed a major [CuH(O(dPro)-Asp)](2+) species (pH range 5.5-7.0), in which the Cu(2+) ion was bound to the His and Asp residues in square-planar or square-pyramidal geometries. The stability constant corrected for protonated species (log K* CuH(O dPro-Asp)=9.33) is almost equal to the value obtained for the parent [CuH(OAsp)](2+) species (log K*CuH(O-Asp) =9.28), but lower than that obtained for the cyclic [CuH(C-Asp)](2+) complex (log K*CuH(C-Asp) =10.79) previously published. Thus, the replacement of the ProGly unit by the stronger β-turn-inducing dProPro unit did not generate a more stable copper(II) species, although the O(dPro)-Asp peptide was structured in solution, as shown by circular dichroism (CD) spectroscopy. Interestingly, the calculated value of Keff showed that this peptide behaved similarly to the O-Asp or C-Asp counterparts, depending on the pH value. The cyclic voltammetry data indicated that the most easily reducible species were [CuH(O-Asp)](2+) (E'(0) =262 mV versus a normal hydrogen electrode (NHE)) and [CuH(O(dPro)-Asp)](2+) (E'(0) =294 mV versus NHE) complexes, the peptidic scaffolds of which are open. A lower value was obtained for [CuH(C-Asp)](2+) (E'(0) =24 mV versus NHE). A different degree of non-reversibility was observed for the three copper(II) complexes; this could reflect a different degree of flexibility in their respective peptidic scaffolds.

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Copper(II), nickel(II) and zinc(II) complexes of N-acetyl-His-Pro-His-His-NH2: Equilibria, solution structure and enzyme mimicking

Cited by 35 publications

References 52 publications

Probing the Cu2+ and Zn2+ binding affinity of histidine-rich glycoprotein

Probing the Cu2+ and Zn2+ binding affinity of histidine-rich glycoprotein

Harnessing the Flexibility of Peptidic Scaffolds to Control their Copper(II)‐Coordination Properties: A Potentiometric and Spectroscopic Study

Effect of the Peptidic Scaffold in Copper(II) Coordination and the Redox Properties of Short Histidine‐Containing Peptides

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