Copper(II) interaction with peptide fragments of histidine–proline-rich glycoprotein: Speciation, stability and binding details

Mendola, Diego La; Magrı̀, Antonio; Santoro, Anna Maria; Nicoletti, Vincenzo Giuseppe; Rizzarelli, Enrico

doi:10.1016/j.jinorgbio.2012.02.027

Cited by 33 publications

(38 citation statements)

References 67 publications

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“…The protonation of the three histidyl residues takes place in an overlapping process. The average value for the protonation of the imidazole nitrogens (pK = 6.27) is close to that of other histidine containing peptides [53,54].…”

Section: Resultssupporting

confidence: 68%

“…The considerably blue shift UV-Vis (λ= 550 nm, ε=109 M -1 cm -1 ) and the Hamiltonian parameter values (Table 4), confirm a 4N coordination mode, as reported for analogous copper(II) complex species which show similar parameters (λ = 550 nm, ε= 112 M -1 cm -1 and g ║ =2.197; A ║ =199 × 10 -4 cm -1 ) [56,57].…”

Section: Speciation Stability Constant and Coordination Environmentssupporting

confidence: 83%

“…However, the UV-Vis parameters extrapolated by titrations (λ max = 655 nm, ε =50 M -1 cm -1 ) are different from those reported for a Cu (2N Im , 2O) binding mode (λ max = 694 nm, ε =35 M -1 cm -1 ) [57], rather suggesting the involvement of one deprotonated amide nitrogen atom together with one imidazole. The presence of an isomer with N Im , N -as donor atoms requires the contemporary protonation of one imidazole nitrogen conceivable at pH 6, taking into account the protonation constant values, so the actual isomer form of [CuHL] is [CuH -1 L(H 2 )].…”

Section: Speciation Stability Constant and Coordination Environmentscontrasting

confidence: 79%

“…The calculated stability constant value (logK = logβ 111 -logβ 011 = 5.62) is indicative of the involvement of two imidazole nitrogen atoms in metal ion coordination, as reported for analogous copper(II) species formed by peptides encompassing two or more histidine residues (logK 111 =5.66) [56,57].…”

Section: Speciation Stability Constant and Coordination Environmentssupporting

confidence: 68%

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The Inorganic Perspective of VEGF: Interactions of Cu2+ with Peptides Encompassing a Recognition Domain of the VEGF Receptor

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Section: Resultssupporting

confidence: 68%

Section: Speciation Stability Constant and Coordination Environmentssupporting

confidence: 83%

Section: Speciation Stability Constant and Coordination Environmentscontrasting

confidence: 79%

Section: Speciation Stability Constant and Coordination Environmentssupporting

confidence: 68%

See 2 more Smart Citations

The Inorganic Perspective of VEGF: Interactions of Cu2+ with Peptides Encompassing a Recognition Domain of the VEGF Receptor

Grasso

Santoro

Magrı̀

et al. 2016

Journal of Inorganic Biochemistry

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“…The studies on the copper(II) complexes of the peptide fragments of prion protein and related substances revealed that the internal histidyl residues can also be anchoring sites for copper(II) or nickel(II) binding [5]. Moreover, the formation of polynuclear copper(II) and/or nickel(II) complexes was observed with various multihistidine peptides [8][9][10][11]. Peptide fragments of prion protein and amyloid-β peptides provided the most evident examples for the binding of more than one copper(II) and nickel(II) ions in these complexes [12][13][14][15][16].…”

Section: Introductionmentioning

confidence: 99%

Binary and ternary mixed metal complexes of terminally free peptides containing two different histidyl binding sites

Grenács

Kaluha

Kállay

et al. 2013

Journal of Inorganic Biochemistry

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Copper, BDNF and Its N‐terminal Domain: Inorganic Features and Biological Perspectives

Travaglia

Mendola

Magrı̀

et al. 2012

Chemistry A European J

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Brain-derived neurotrophic factor (BDNF) is a neurotrophin that influences development, maintenance, survival, and synaptic plasticity of central and peripheral nervous systems. Altered BDNF signaling is involved in several neurodegenerative disorders including Alzheimer's disease. Metal ions may influence the BDNF activity and it is well known that the alteration of Cu(2+) homeostasis is a prominent factor in the development of neurological pathologies. The N-terminal domain of BDNF represents the recognition site of its specific receptor TrkB, and metal ions interaction with this protein domain may influence the protein/receptor interaction. In spite of this, no data inherent the interaction of BDNF with Cu(2+) ions has been reported up to now. Cu(2+) complexes of the peptide fragment BDNF(1-12) encompassing the sequence 1-12 of N-terminal domain of human BDNF protein were characterized by means of potentiometry, spectroscopic methods (UV/Vis, CD, EPR), parallel tempering simulations and DFT-geometry optimizations. Coordination features of the acetylated form, Ac-BDNF(1-12), were also characterized to understand the involvement of the terminal amino group. Whereas, an analogous peptide, BDNF(1-12)D3N, in which the aspartate residue was substituted by an asparagine, was synthesized to provide evidence on the possible role of carboxylate group in Cu(2+) coordination. The results demonstrated that the amino group is involved in metal binding and the metal coordination environment of the predominant complex species at physiological pH consisted of one amino group, two amide nitrogen atoms, and one carboxylate group. Noteworthy, a strong decrease of the proliferative activity of both BDNF(1-12) and the whole protein on a SHSY5Y neuroblastoma cell line was found after treatment in the presence of Cu(2+). The effect of metal addition is opposite to that observed for the analogous fragment of nerve growth factor (NGF) protein, highlighting the role of specific domains, and suggesting that Cu(2+) may drive different pathways for the BDNF and NGF in physiological as well as pathological conditions.

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Copper(II) interaction with peptide fragments of histidine–proline-rich glycoprotein: Speciation, stability and binding details

Cited by 33 publications

References 67 publications

The Inorganic Perspective of VEGF: Interactions of Cu2+ with Peptides Encompassing a Recognition Domain of the VEGF Receptor

The Inorganic Perspective of VEGF: Interactions of Cu2+ with Peptides Encompassing a Recognition Domain of the VEGF Receptor

Binary and ternary mixed metal complexes of terminally free peptides containing two different histidyl binding sites

Copper, BDNF and Its N‐terminal Domain: Inorganic Features and Biological Perspectives

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