Competition of zinc(II) with cadmium(II) or mercury(II) in binding to a 12-mer peptide

Jancsó, Attila; Gyurcsik, Béla; Mesterházy, Edit; Berkecz, Róbert

doi:10.1016/j.jinorgbio.2013.05.019

Cited by 25 publications

(29 citation statements)

References 70 publications

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“…[7][8][9][10] Peptide models contribute to the understanding of mercury coordination in water related to Hg(II) ability to bind sulfur proteins and therefore to its toxicity. Linear model peptides with 2 binding cysteines in their sequences have been studied to mimic the transport proteins MerP [11][12][13] and MerT 14 or Cu regulators 15,16 and induce the stable linear HgS2 environment. Constrained peptides have been developed to mimic the role of the whole protein structure in short sequences.…”

Section: Introductionmentioning

confidence: 99%

Mercury Trithiolate Binding (HgS₃) to a de Novo Designed Cyclic Decapeptide with Three Preoriented Cysteine Side Chains

et al. 2018

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Mercury(II) is an unphysiological soft ion with high binding affinity for thiolate ligands. Its toxicity lies in the interactions with low molecular weight thiols including glutathione and cysteine-containing proteins that disrupt the thiol balance and alter vital functions. However, mercury can also be detoxified via interactions with Hg(II)-responsive regulatory proteins such as MerR, which coordinates Hg(II) with three cysteine residues in a trigonal planar fashion (HgS coordination). The model cyclodecapeptide P, c(GCTCSGCSRP) was designed to promote Hg(II) chelation in a HgS coordination environment through the parallel orientation of three cysteine side chains. The binding motif is derived from the dicysteine P cyclodecapeptide validated previously as a model for d metal transporters containing the binding sequence CxxC. The formation of the mononuclear HgP complex with a HgS coordination is demonstrated using electrospray ionization mass spectrometry, UV absorption, and Hg NMR. Hg L-edge extended X-ray absorption fine structure (EXAFS) spectroscopy indicates that the Hg(II) coordination environment is T-shaped with two short Hg-S distances at 2.45 Å and one longer distance at 2.60 Å. The solution structure of the HgP complex was refined based on H-H NMR constraints and EXAFS results. The cyclic peptide scaffold has a rectangular shape with the three binding cysteine side chains pointing toward Hg(II). The HgPH complex has a p K of 4.3, indicating that the HgS coordination mode is stable over a large range of pH. This low p K value suggests that the preorientation of the three cysteine groups is particularly well-achieved for Hg(II) trithiolate coordination in P.

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Section: Introductionmentioning

confidence: 99%

Mercury Trithiolate Binding (HgS₃) to a de Novo Designed Cyclic Decapeptide with Three Preoriented Cysteine Side Chains

et al. 2018

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“…28 The major result of our studies on the various metal ionoligopeptide systems is a finding that the model ligands possess fundamentally distinct binding features for the monovalent ion Ag + and the divalent ions Zn 2+ , Cd 2+ and Hg 2+ . [29][30][31][32] The binding of Ag + to the ligands under acidic conditions (even at pH = 2) was proved by UV-, CD-and 1 H-NMR experiments, as well as pH-potentiometric titrations ( Figure 6). 31 Spectroscopic data suggest the coordination of at least one of the Cys-sidechain donors as a thiolate to Ag + in the Ag + -PP 1:1 system (PP = Ac-SCPGDQGSDCPI-NH 2 ).…”

Section: Hivatkozásokmentioning

confidence: 93%

Metalloproteinek fémkötőhelyein alapuló oligopeptidek, mint potenciális toxikus fémion érzékelők

Szekeres¹,

Szunyogh²,

Galbács³

et al. 2017

MKF

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“…hydrogen ion concentrations was done by a method described in one of our earlier publications. 34 The protonation and complex formation equilibria of the immobilized ligand were characterized by the following general equilibrium process:…”

Section: Peptide Synthesis On Silica Surfacesmentioning

confidence: 99%

“…The metal-ion binding features of several short oligopeptides, containing two cysteine residues, have already been investigated in our group from different perspectives. 33,34 The studied 12-mer oligopeptide ligands proved to coordinate the studied group-12 metal ions (Zn(II), Cd(II) and Hg(II)) rather efficiently. Reports discussing the heavy metal ion binding capabilities of similar compounds, such as cysteine and poly-L-cysteine, 35,36 as well as poly-L-aspartate, 37 coupled to various solid supports (e.g.…”

Section: Introductionmentioning

confidence: 99%

Cd(II) Capture Ability of an Immobilized, Fluorescent Hexapeptide

Galbács

Szokolai

Kormányos

et al. 2015

Bulletin of the Chemical Society of Japan

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Cys-Tyr-(YY), targeting Cd(II) ion sensing, was synthesized on various solid supports including two resins, as well as glass and quartz surfaces. The synthesis was based on the Fmoc (9-fluorenylmethoxycarbonyl) and the APTES (3-aminopropyltriethoxysilane) methodologies on the resin and silica supports, respectively. The immobilized ligand, except when coupled to a hydrophobic benzhydrylamine resin, showed a remarkably efficient, pHdependent Cd(II) capturing ability with a maximum binding capacity around neutral pH. The effect of contact time and metal ion concentration was also studied with a hydrophilic resin supported peptide (YY-NTG). The interaction of YY-NTG with Cd(II) was investigated by pH-potentiometric titrations in aqueous samples containing the resin beads and Cd(II). These studies, together with metal ion capturing experiments under buffer-controlled pH, prove that each immobilized peptide can bind one Cd(II) ion at pH=7.0 in the presence of one equivalent metal ion or metal ion excess. For Cd(II) binding to YY-NTG a notably high, K=1.310 10 apparent stability constant was determined (1:1 metal-to-ligand ratio, pH=7.0). Analytical results suggests that the concentration of Cd(II) can be measured below 200 nM with this silica-supported peptide. The usefulness of the probe was demonstrated by fluorescence spectroscopy.

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Competition of zinc(II) with cadmium(II) or mercury(II) in binding to a 12-mer peptide

Abstract: Speciation of the complexes of zinc(II) with a dodecapeptide (Ac-SCPGDQGSDCSI-

Cited by 25 publications

References 70 publications

Mercury Trithiolate Binding (HgS₃) to a de Novo Designed Cyclic Decapeptide with Three Preoriented Cysteine Side Chains

Mercury Trithiolate Binding (HgS₃) to a de Novo Designed Cyclic Decapeptide with Three Preoriented Cysteine Side Chains

Metalloproteinek fémkötőhelyein alapuló oligopeptidek, mint potenciális toxikus fémion érzékelők

Cd(II) Capture Ability of an Immobilized, Fluorescent Hexapeptide

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Competition of zinc(II) with cadmium(II) or mercury(II) in binding to a 12-mer peptide

Abstract: Speciation of the complexes of zinc(II) with a dodecapeptide (Ac-SCPGDQGSDCSI-

Cited by 25 publications

References 70 publications

Mercury Trithiolate Binding (HgS3) to a de Novo Designed Cyclic Decapeptide with Three Preoriented Cysteine Side Chains

Mercury Trithiolate Binding (HgS3) to a de Novo Designed Cyclic Decapeptide with Three Preoriented Cysteine Side Chains

Metalloproteinek fémkötőhelyein alapuló oligopeptidek, mint potenciális toxikus fémion érzékelők

Cd(II) Capture Ability of an Immobilized, Fluorescent Hexapeptide

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Product

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Mercury Trithiolate Binding (HgS₃) to a de Novo Designed Cyclic Decapeptide with Three Preoriented Cysteine Side Chains

Mercury Trithiolate Binding (HgS₃) to a de Novo Designed Cyclic Decapeptide with Three Preoriented Cysteine Side Chains