Coordination properties of Cu(II) and Ni(II) ions towards the C-terminal peptide fragment –ELAKHA– of histone H2B

Karavelas, Tilemachos; Mylonas, Marios; Malandrinos, Gerasimos; Plakatouras, John C.; Hadjiliadis, Nick; Młynarz, Piotr; Kozłowski, Henryk

doi:10.1016/j.jinorgbio.2004.11.012

Cited by 37 publications

(59 citation statements)

References 27 publications

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“…AcNGFA C H T U N G T R E N N U N G (1-14) does not complex Cu 2 + up to pH 4; at this pH value [CuL'] + starts to form and reaches its maximum percentage at pH 5 ( Figure 6a). The stability constant (log K = 6.37) is two logarithmic units larger than that of similar Cu 2 + complexes of peptide fragments in which the metal centre forms a macrochelate with an N im and COO À binding mode, [35,36] whereas it is similar to that reported for Ab peptide fragments for which metal ions have been shown to form a macrochelate with a 2 N im , COO À coordination environment (log K = 6.18). [37] This suggests that two histidine imidazole nitrogen atoms and the glutamate carboxylate group are involved in Cu 2 + binding to AcNGFA C H T U N G T R E N N U N G (1-14).…”

Section: Speciessupporting

confidence: 58%

The Inorganic Perspective of Nerve Growth Factor: Interactions of Cu²⁺ and Zn²⁺ with the N‐Terminus Fragment of Nerve Growth Factor Encompassing the Recognition Domain of the TrkA Receptor

Travaglia

Arena

Fattorusso³

et al. 2011

Chemistry A European J

101

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There is a significant overlap between brain areas with Zn(2+) and Cu(2+) pathological dys-homeostasis and those in which the nerve growth factor (NGF) performs its biological role. The protein NGF is necessary for the development and maintenance of the sympathetic and sensory nervous systems. Its flexible N-terminal region has been shown to be a critical domain for TrkA receptor binding and activation. Computational analyses show that Zn(2+) and Cu(2+) form pentacoordinate complexes involving both the His4 and His8 residues of the N-terminal domain of one monomeric unit and the His84 and Asp105 residues of the other monomeric unit of the NGF active dimer. To date, neither experimental data on the coordination features have been reported, nor has one of the hypotheses according to which Zn(2+) and Cu(2+) may have different binding environments or the Ser1 α-amino group could be involved in coordination been supported. The peptide fragment, encompassing the 1-14 sequence of the human NGF amino-terminal domain (NGF(1-14)), blocked at the C terminus, was synthesised and its Cu(2+) and Zn(2+) complexes characterized by means of potentiometric and spectroscopic (UV/Vis, CD, NMR, and EPR) techniques. The N-terminus-acetylated form of NGF(1-14) was also investigated to evaluate the involvement of the Ser1 α-amino group in metal-ion coordination. Our results demonstrate that the amino group is the first anchoring site for Cu(2+) and is involved in Zn(2+) coordination at physiological pH. Finally, a synergic proliferative activity of both NGF(1-14) and the whole protein on SHSY5Y neuroblastoma cell line was found after treatment in the presence of Cu(2+). This effect was not observed after treatment with the N-acetylated peptide fragment, demonstrating a functional involvement of the N-terminal amino group in metal binding and peptide activity.

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Section: Speciessupporting

confidence: 58%

The Inorganic Perspective of Nerve Growth Factor: Interactions of Cu²⁺ and Zn²⁺ with the N‐Terminus Fragment of Nerve Growth Factor Encompassing the Recognition Domain of the TrkA Receptor

Travaglia

Arena

Fattorusso³

et al. 2011

Chemistry A European J

101

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“…Table 2. The results are in agreement with other reported data that d-d transitions have absorptions at the said wavelength with molar absorptivity in the range of about 2 -3 Lcm -1 mol -1 [5] and the charge transfer bands (CT bands) for copper bound peptides normally have similar or lower molar absorptivity than that of d-d transition bands and appear in the range of 400 -600 nm [6].…”

Section: Fmoc-fluorenylmethyloxycarbonyl Chloridesupporting

confidence: 93%

Spectroscopic Characterization of Copper(ii)-Based Tetrapeptides

Rahman¹,

Begum²,

Tahir³

et al. 2016

MJAS

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Five different histidine and aspartic acid based tetrapeptides were designed using LOMETS and PyMol. They were chemically synthesized following the solid phase Fmoc-peptide synthesis protocols and were analysed using the reverse-phase High Performance Liquid Chromatography (HPLC) C 18 analytical column for the purity. The peptides were further analysed by Liquid Chromatography Mass Spectrometry (LCMS) to see if the desired peptides were synthesized systematically. Copper(II) acetate monohydrate was bound to the peptides and the best molar ratio for the binding of these metal salts to peptides was 2:1. These observations were monitored through several spectroscopic techniques. The first physical observations for the successful synthesis of metallopeptides were the colour change, the melting/decomposition points and the solubility of these metallopeptides. Due to the visible colour change of the peptides to metallopeptides, UV-Visible spectroscopy and UVFluorescence spectroscopy were used as a qualitative analysis tests and the results were in agreement with other researchers' data from similar researches.Keywords: copper(II), histidine, aspartic acid, tetrapeptides, spectroscopic Abstrak Lima tetrapeptida berbeza yang mempunyai histidine dan asid aspartik direkabentuk oleh LOMETS dan PyMol. Tetrapeptida ini disintesis mengikut skim fasa pepejal peptida dan dianalisis menggunakan fasa sonsang Kromatografi Cecair Berprestasi Tinggi (HPLC) C 18 turus analisis untuk mengetahui keaslian peptida. Kesemua peptida ini dianalisis mengunakan Kromatografi CecairSpektrometer Jisim (LC-MS) untuk mengkaji sintesis peptida secara sistematik. Kuprum(II) asetat monohidrat terikat kepada peptida dan nisbah mol yang terbaik untuk mengikat garam logam ini kepada peptida adalah 2:1. Cerapan ini telah dipantau melalui beberapa teknik spektroskopi. Pemerhatian fizikal pertama untuk logam peptida yang berjaya disintesis ialah perubahan warna, takat lebur/penguraian dan kebolehlarutan peptida logam ini. Oleh kerana perubahan warna yang nyata dalam dari peptida kepada logam peptida, spektroskopi Ultralembayung-tampak (UV-Vis) dan spektroskopi Ultralembayung-Pendafluor (UVFluorescence) digunakan sebagai ujian analisis kuantatif dan data yang diperolehi adalah setara dengan perolehan data bagi penyelidikan yang serupa.Kata kunci: Kuprum(II), histidin, asid aspartik, tetrapeptida, spektroskopi ISSN -2506 Mohd. Basyaruddin et al: SPECTROSCOPIC CHARACTERIZATION OF COPPER(II)-BASED TETRAPEPTIDES 736Introduction Metallopeptides that are easier and cheaper to synthesise when compared to metalloproteins have caught the attention of many researchers. Metallopeptides, synthesized from metal salt and peptides, are known as pseudoproteins. They imitate the applications of large proteins especially in the industrial field of catalysis as well as in biological applications [1]. Metallopeptides are hybrid structures that combine peptides and metal and in this project, the transition metal copper(II) was used, that has various roles when used as b...

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“…[75][76][77] Interestingly, nickel has been shown to form a stable complex with the C-terminal ELAKHA hexapeptide of H2B. 78 Currently, the mechanism of peptide cleavage and its biological significance remain elusive.…”

Section: O N O T D I S T R I B U T Ementioning

confidence: 99%

Environmental epigenetics in metal exposure

2011

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Coordination properties of Cu(II) and Ni(II) ions towards the C-terminal peptide fragment –ELAKHA– of histone H2B

Cited by 37 publications

References 27 publications

The Inorganic Perspective of Nerve Growth Factor: Interactions of Cu²⁺ and Zn²⁺ with the N‐Terminus Fragment of Nerve Growth Factor Encompassing the Recognition Domain of the TrkA Receptor

The Inorganic Perspective of Nerve Growth Factor: Interactions of Cu²⁺ and Zn²⁺ with the N‐Terminus Fragment of Nerve Growth Factor Encompassing the Recognition Domain of the TrkA Receptor

Spectroscopic Characterization of Copper(ii)-Based Tetrapeptides

Environmental epigenetics in metal exposure

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Coordination properties of Cu(II) and Ni(II) ions towards the C-terminal peptide fragment –ELAKHA– of histone H2B

Cited by 37 publications

References 27 publications

The Inorganic Perspective of Nerve Growth Factor: Interactions of Cu2+ and Zn2+ with the N‐Terminus Fragment of Nerve Growth Factor Encompassing the Recognition Domain of the TrkA Receptor

The Inorganic Perspective of Nerve Growth Factor: Interactions of Cu2+ and Zn2+ with the N‐Terminus Fragment of Nerve Growth Factor Encompassing the Recognition Domain of the TrkA Receptor

Spectroscopic Characterization of Copper(ii)-Based Tetrapeptides

Environmental epigenetics in metal exposure

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Product

Resources

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The Inorganic Perspective of Nerve Growth Factor: Interactions of Cu²⁺ and Zn²⁺ with the N‐Terminus Fragment of Nerve Growth Factor Encompassing the Recognition Domain of the TrkA Receptor

The Inorganic Perspective of Nerve Growth Factor: Interactions of Cu²⁺ and Zn²⁺ with the N‐Terminus Fragment of Nerve Growth Factor Encompassing the Recognition Domain of the TrkA Receptor