The His–His sequence of the antimicrobial peptide demegen P-113 makes it very attractive ligand for Cu2+

Kulon, Kinga; Valensin, Daniela; Kamysz, Wojciech; Valensin, Gianni; Nadolski, Piotr; Porciatti, Elena; Gaggelli, Elena; Kozłowski, Henryk

doi:10.1016/j.jinorgbio.2007.12.021

Cited by 28 publications

(30 citation statements)

References 42 publications

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“…The UV-vis and EPR parameters (Table 2) support macrochelate formation with the presence of a Cu(2N Im , O carbonyl , O water ) chromophore, as observed in similar peptides encompassing two vicinal histidine residues [35,37]. The percentage formation of [CuL] 2+ was a maximum at pH 5.8.…”

Section: Resultssupporting

confidence: 57%

Copper Binding Features of Tropomyosin-Receptor-Kinase-A Fragment: Clue for Neurotrophic Factors and Metals Link

Magrı̀

Mendola

2018

IJMS

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The nerve growth factor (NGF) is a neurotrophin essential for the development and maintenance of neurons, whose activity is influenced by copper ions. The NGF protein exerts its action by binding to its specific receptor, TrkA. In this study, a specific domain of the TrkA receptor, region 58–64, was synthesized and its copper(II) complexes characterized by means of potentiometric and spectroscopic studies. The two vicinal histidine residues provide excellent metal anchoring sites and, at physiological pH, a complex with the involvement of the peptide backbone amide nitrogen is the predominant species. The TrkA peptide is competitive for metal binding with analogous peptides due to the N-terminal domain of NGF. These data provide cues for future exploration of the effect of metal ions on the activity of the NGF and its specific cellular receptor.

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Section: Resultssupporting

confidence: 57%

Copper Binding Features of Tropomyosin-Receptor-Kinase-A Fragment: Clue for Neurotrophic Factors and Metals Link

Magrı̀

Mendola

2018

IJMS

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“…However, NMR data strongly suggest, that imidazole nitrogen of His-12 can complete the donor set in apical position (Fig. 17) [59]. The significance of two adjacent His was proven by the comparison of the binding efficacies of DMG-NH 2 and H5A-DMG-NH 2 , where around pH 5-6 very considerable differences in binding ability are seen with the parent peptide being much more effective in metal ion coordination.…”

Section: Coordination Properties Of Demegen P-113 Towards Cu 2+ Ionsmentioning

confidence: 95%

“…16) [59]. Comparison of the parent DMG-NH 2 with the modified peptides with H5A and H12A mutations shows that His residues are of critical importance during the complex formation, particularly at pH range 4.5-6.…”

Section: Coordination Properties Of Demegen P-113 Towards Cu 2+ Ionsmentioning

confidence: 99%

Specificity in the Cu2+ interactions with prion protein fragments and related His-rich peptides from mammals to fishes

Kozłowski

Janicka-Kłos²,

Stańczak³

et al. 2008

Coordination Chemistry Reviews

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“…The average value for the protonation of the imidazole nitrogens (pK = 6.39) is very close to that of other histidine containing peptides but lower than that obtained for hAng (10−17). 31,32 The protonation processes of Tyr-6, Tyr-14, and Lys-17 also take place in an overlapping equilibrium, thus each protonation constant value should be considered as a macroconstant. The presence of different networks of side-chain interactions could be the origin of some differences in the pK values among the investigated peptides.…”

Section: ■ Experimental Sectionmentioning

confidence: 99%

Probing the Copper(II) Binding Features of Angiogenin. Similarities and Differences between a N-Terminus Peptide Fragment and the Recombinant Human Protein

et al. 2011

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The angiogenin protein (hAng) is a potent angiogenic factor and its cellular activities may be affected by copper ions even if it is yet unknown how this metal ion is able to produce this effect. Among the different regions of hAng potentially able to bind copper ions, the N-terminal domain appears to be an ideal candidate. Copper(II) complexes of the peptide fragments encompassing the amino acid residues 4-17 of hAng protein were characterized by potentiometric, UV-vis, CD, and EPR spectroscopic methods. The results show that these fragments have an unusual copper(II) binding ability. At physiological pH, the prevailing complex species formed by the peptide encompassing the protein sequence 4-17 is [CuHL], in which the metal ion is bound to two imidazole and two deprotonated amide nitrogen atoms disposed in a planar equatorial arrangement. Preliminary spectroscopic (UV-vis, CD, and EPR) data obtained on the copper(II) complexes formed by the whole recombinant hAng protein, show a great similarity with those obtained for the N-terminal peptide fragments. These findings indicate that within the N-terminal domain there is one of the preferred copper(II) ions anchoring site of the whole recombinant hAng protein.

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The His–His sequence of the antimicrobial peptide demegen P-113 makes it very attractive ligand for Cu2+

Cited by 28 publications

References 42 publications

Copper Binding Features of Tropomyosin-Receptor-Kinase-A Fragment: Clue for Neurotrophic Factors and Metals Link

Copper Binding Features of Tropomyosin-Receptor-Kinase-A Fragment: Clue for Neurotrophic Factors and Metals Link

Specificity in the Cu2+ interactions with prion protein fragments and related His-rich peptides from mammals to fishes

Probing the Copper(II) Binding Features of Angiogenin. Similarities and Differences between a N-Terminus Peptide Fragment and the Recombinant Human Protein

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