Spectroscopic and potentiometric evidence for the stabilization of a bent structure of octapeptides by Cu(II) ions

Bataille, Michel; Pettit, Leslie D.; Steel, Ian; Kozłowski, Henryk; Tatarowski, Tomasz

doi:10.1016/0162-0134(85)85004-2

Cited by 18 publications

(1 citation statement)

References 9 publications

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“…There is an enormous structural variety for the complex formation of prolyl and weakly or strongly coordinating side chain residues [248][249][250][251][252]. The most interesting feature of systems containing proline residues is the induction of large macrochelate loops formation, with Cu 2+ bound to the N-terminal amino group and a distance donor.…”

Section: Impact Of Proline On Peptide Coordination Abilitiesmentioning

confidence: 99%

Study of the mechanisms of toxicity and carcinogenicity induced by metal ions

Nunes¹

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European Social Fund), with the title "Study of the mechanisms of toxicity and carcinogenicity induced by metal ions" and coordinated by Prof. Nick Hadjiliadis. The subject of the thesis was given to me by Prof. N. Hadjiliadis and the thesis was performed mainly in his laboratory.I would like therefore, first to thank Prof. Nick Hadjiliadis, my supervisor, for the opportunity he gave me, by organizing every step of the thesis, the support both financial and scientific, and guidance and in summary for providing me with all necessary tools for the development and successful ending of this work.

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Section: Impact Of Proline On Peptide Coordination Abilitiesmentioning

confidence: 99%

Study of the mechanisms of toxicity and carcinogenicity induced by metal ions

Nunes¹

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Peptide–Metal InteractionsBased in part on the article Peptide–Metal Interactions by Justin K. Moran & Claude F. Meares which appeared in the Encyclopedia of Inorganic Chemistry, First Edition .

Meares

2005

Encyclopedia of Inorganic Chemistry

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Copper–peptide complexes have been the most extensively studied of all the metal–peptide complexes. Copper(II) is the most important oxidation state in copper–peptide complexes, although copper(III) can be stabilized by coordination to peptides. The deprotonated peptide nitrogens help stabilize the higher oxidation state of copper; therefore the more deprotonated peptide nitrogens, the more stable the copper(III) complex. The copper(II) complexes of GlyGlyProGly and (GlyGlyProGly)2 are very similar. At low pH, both peptides bond through the amino nitrogen and carbonyl oxygen of the first peptide linkage. The peptides GlyGlyProLys and (GlyGlyProLys)2 initially form 1N complexes with copper(II). With luteinizing hormone‐releasing hormone the copper(II) is coordinated via the imidazole nitrogen and two deprotonated peptide nitrogens. With angiotensin II, the copper(II) is bonded via the imidazole nitrogen of the histidine residue and two deprotonated peptide nitrogens. The dipeptide TyrPro bonded copper(II) through the amino nitrogen and the peptide carbonyl. Since there was no ionizable hydrogen on the peptide nitrogen, there was no bonding by the peptide nitrogen. The copper(II)AVP (vasopressin analog) complex is one of the most stable 4N copper–peptide complexes known. Owing to their similarities, nickel(II)–peptide complexes are usually studied along with copper(II) complexes. In neutral to acidic solutions, the nickel is coordinated through the amino nitrogen and the carbonyl oxygen (1N). When the pH is raised to 9.0, nickel(II) substitutes for a peptide hydrogen, and the coordination changes. In NiH1L complexes of cysteine‐containing dipeptides, the nickel is coordinated via the amino and deprotonated peptide nitrogens and the thiol group. Zinc‐peptide complexes are less stable. With the dipeptides Ala–His and Gly–His at high pH, zinc(II) was shown to form complexes coordinated through the amino nitrogen, deprotonated peptide nitrogen, and the imidazole nitrogen. Unlike copper(II), both palladium(II) and platinum(II) are soft acceptors and as such are expected to coordinate to soft donors like sulfur and aromatic nitrogen donors in residues such as Met and His, and deprotonated peptide nitrogens. Early investigations of metals showed that divalent metals such as copper(II), cobalt(II), and nickel(II) could catalyze the hydrolysis of amino acid esters. Mechanisms of cobalt(III)‐mediated peptide‐bond cleavage have been investigated; because cobalt(III) complexes bind to the N‐terminal amino acid residue of peptides, only the N‐terminal peptide bond is hydrolyzed. Complexes containing iron can cleave peptide bonds, as can complexes of palladium or platinum.

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Metal Ion Effects on the cis/trans Isomerization Equilibrium of Proline in Short-Chain Peptides: A Solution NMR Study

et al. 2001

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The effect of copper(II) ions on the probabilities of existence of the four detectable conformers of the tetrapeptide Tyr-Pro-Phe-Pro (beta-casomorphin 4) in [2H6]DMSO was investigated by 1H NMR spectroscopy. Integration of the Phe-NH signals provided the relative populations in the free state as tt/tc/ct/cc=28:34:29:9 at 293 K (c=cis, t=trans). Copper(II) was shown to bind to all four isomers, yielding complexes with two different structures, depending on the conformation of Pro(2). The interpretation of paramagnetic relaxation rates of Pro(2)-Halpha signals provided the corresponding isomeric probabilities in the metal-bound state as 13:36:20:31. The observed stabilization of the conformation with the lowest probability of existence (cc) may be relevant for the biological role of copper and other metal ions.

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Spectroscopic and potentiometric evidence for the stabilization of a bent structure of octapeptides by Cu(II) ions

Cited by 18 publications

References 9 publications

Study of the mechanisms of toxicity and carcinogenicity induced by metal ions

Study of the mechanisms of toxicity and carcinogenicity induced by metal ions

Peptide–Metal InteractionsBased in part on the article Peptide–Metal Interactions by Justin K. Moran & Claude F. Meares which appeared in the Encyclopedia of Inorganic Chemistry, First Edition .

Metal Ion Effects on the cis/trans Isomerization Equilibrium of Proline in Short-Chain Peptides: A Solution NMR Study

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