Stability constants of bio-relevant, redox-active metals with amino acids: The challenges of weakly binding ligands

Murphy, Jaime M.; Powell, Brian A.; Brumaghim, Julia L.

doi:10.1016/j.ccr.2020.213253

Cited by 32 publications

(25 citation statements)

References 206 publications

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“…We suspect that the thermodynamically favored formation of copper‐Hcy complexes or precipitates is the major driving force for the observed selectivity for Hcy over Cys in the disassembly process of 1 . In fact, Hcy has a higher copper(II) stability constant (Cu II (Hcy); log β=11.92(1)) [18] than all proteinogenic amino acids including Cys [19] . At present, we were not able to isolate or identify copper‐containing reaction products and, hence, a redox‐triggered disassembly process between copper(II) and biothiols to copper(I) and disulfides cannot be excluded [18,20] …”

Section: Resultsmentioning

confidence: 87%

“…In fact, Hcy has a higher copper(II) stability constant (Cu II (Hcy); log β=11.92(1)) [18] than all proteinogenic amino acids including Cys. [19] At present, we were not able to isolate or identify copper‐containing reaction products and, hence, a redox‐triggered disassembly process between copper(II) and biothiols to copper(I) and disulfides cannot be excluded. [ 18 , 20 ]…”

Section: Resultsmentioning

confidence: 99%

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A Cu^II‐Salicylidene Glycinato Complex for the Selective Fluorometric Detection of Homocysteine over 20 Proteinogenic Amino Acids

Yadav

Spingler

et al. 2022

ChemistryOpen

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Homocysteine (Hcy) is a sulfur-containing α-amino acid that differs by one methylene (CH 2 ) subunit from homologous cysteine (Cys). Elevated levels of Hcy are diagnostic markers of cardiovascular disease and other medical conditions. We present a new Cu II -salicylidene glycinato complex 1 for the selective fluorometric detection of Hcy in water. In the presence of this analyte, the non-fluorescent copper-complex demetallates and disassembles into its building blocks. This process liberates a 3-chloro-5-sulfosalicylaldehyde signaling unit and is accompanied by a 51-fold turn-on fluorescence at 485 nm (λ ex = 350 nm). Out of twenty proteinogenic amino acids, only histidine (12-fold turn-on fluorescence) and Cys (8-fold turn-on fluorescence) trigger some disassembly of probe 1. In comparison with important pioneering work on the detection of biothiols, this study strikingly demonstrates that structural modifications of chelate core structures steer substrate selectivity of metal-based probes. Importantly, probe 1 has proven suitable for the detection of Hcy in artificial urine.

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Section: Resultsmentioning

confidence: 87%

Section: Resultsmentioning

confidence: 99%

A Cu^II‐Salicylidene Glycinato Complex for the Selective Fluorometric Detection of Homocysteine over 20 Proteinogenic Amino Acids

Yadav

Spingler

et al. 2022

ChemistryOpen

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“…However, the direct comparison between the stability constant values cannot provide the indication on which peptide binds metal ions more strongly since, as discussed above, they can form complex species with different deprotonation state [ 65 ]. For this reason, the apparent dissociation constant,

, is often used to describe, in the biological field, the affinity of a metal to a protein or a peptide.…”

Section: Discussionmentioning

confidence: 99%

Nerve Growth Factor Peptides Bind Copper(II) with High Affinity: A Thermodynamic Approach to Unveil Overlooked Neurotrophin Roles

Magrı̀

Mendola

Rizzarelli

2021

IJMS

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Nerve growth factor (NGF) is a protein essential to neurons survival, which interacts with its receptor as a non-covalent dimer. Peptides belonging to NGF N-terminal domain are able to mimic the activity of the whole protein. Such activity is affected by the presence of copper ions. The metal is released in the synaptic cleft where proteins, not yet identified, may bind and transfer to human copper transporter 1 (hCtr1), for copper uptake in neurons. The measurements of the stability constants of copper complexes formed by amyloid beta and hCtr1 peptide fragments suggest that beta-amyloid (Aβ) can perform this task. In this work, the stability constant values of copper complex species formed with the dimeric form of N-terminal domain, sequence 1–15 of the protein, were determined by means of potentiometric measurements. At physiological pH, NGF peptides bind one equivalent of copper ion with higher affinity of Aβ and lower than hCtr1 peptide fragments. Therefore, in the synaptic cleft, NGF may act as a potential copper chelating molecule, ionophore or chaperone for hCtr1 for metal uptake. Copper dyshomeostasis and mild acidic environment may modify the balance between metal, NGF, and Aβ, with consequences on the metal cellular uptake and therefore be among causes of the Alzheimer’s disease onset.

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“…The literature survey of the past few years reveals the fact that a signifi cant development in the fi eld of biological activity of metal chelates plays a vital role in the case and treatment of cancer [13][14][15][16] . Metal complexes of carboxylic acids have been studied extensively 17, 18 , but there are not any works on complexes of deoxycholic acid. A clear understanding of the structure and spectroscopic properties of metal complexes usable for their biological applications is the aim of the present work.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and spectroscopic interpretations of Co(II), Ni(II) and Cu(II) decxycholate complexes with molecular docking of COVId-19 protease

Refat

Bakare

Altalhi

et al. 2021

Polish Journal of Chemical Technology

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Co(II), Ni(II) and Cu(II) decxycholate complexes are interesting due to their biologically active and deliberate interest in the research due to their coordination properties. The microanalytical ‘elemental analysis’, molar conductivity, (infrared and Raman) spectroscopy, thermal analyses (TGA/DSC), UV-vis spectra, and ESR for copper(II) decxycholate complex investigations were performed in the structural assignments of Co(II), Ni(II) and Cu(II) decxycholate complexes. Reaction of the sodium deoxycholate ligand (C24H39O4Na) with three transition metal ions form the complexes of formulae, [M(C24H39O4)2(H2O)2]. xH2O where M = Co(II), Ni(II) and Cu(II) where x = 2 for Cu(II) and x = 4 in case of M = Co(II) or Ni(II) metal ions. The FTIR spectra of the complexes show that decxycholate molecule is present as bidentate ligand. Molecular docking utilizing to additionally examine the interaction of COVID-19 (6LU7) with different complexes of deoxycholic acid with Co(II), Ni(II) and Cu(II). Furthermore, in the case of Co(II) deoxycholate complex, the probe is surrounded by amino residues Met235, Pro241, Glu240, Pro108, Gln110, Phe294, and Ile152. The probe molecule of Ni(II) deoxycholate complex is sited close to amino acids Tyr126, Tyr239, Leu287, Leu272, and Lys137. For, Cu(II) deoxycholate complex, the residues of amino acids comprise of Pro132, Pro108, Gln110, Gly109, Ile200, Asn203, Val202, His246, Pro293 and Tyr154. The binding energy was determined from the docking reads for Co(II)–6LU7, Ni(II)–6LU7 and Cu(II)–6LU7 deoxycholate compounds were found to be −446.99, −500.52, −398.13 kcal mol−1 individually.

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Stability constants of bio-relevant, redox-active metals with amino acids: The challenges of weakly binding ligands

Cited by 32 publications

References 206 publications

A Cu^II‐Salicylidene Glycinato Complex for the Selective Fluorometric Detection of Homocysteine over 20 Proteinogenic Amino Acids

A Cu^II‐Salicylidene Glycinato Complex for the Selective Fluorometric Detection of Homocysteine over 20 Proteinogenic Amino Acids

Nerve Growth Factor Peptides Bind Copper(II) with High Affinity: A Thermodynamic Approach to Unveil Overlooked Neurotrophin Roles

Synthesis and spectroscopic interpretations of Co(II), Ni(II) and Cu(II) decxycholate complexes with molecular docking of COVId-19 protease

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Stability constants of bio-relevant, redox-active metals with amino acids: The challenges of weakly binding ligands

Cited by 32 publications

References 206 publications

A CuII‐Salicylidene Glycinato Complex for the Selective Fluorometric Detection of Homocysteine over 20 Proteinogenic Amino Acids

A CuII‐Salicylidene Glycinato Complex for the Selective Fluorometric Detection of Homocysteine over 20 Proteinogenic Amino Acids

Nerve Growth Factor Peptides Bind Copper(II) with High Affinity: A Thermodynamic Approach to Unveil Overlooked Neurotrophin Roles

Synthesis and spectroscopic interpretations of Co(II), Ni(II) and Cu(II) decxycholate complexes with molecular docking of COVId-19 protease

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Product

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A Cu^II‐Salicylidene Glycinato Complex for the Selective Fluorometric Detection of Homocysteine over 20 Proteinogenic Amino Acids

A Cu^II‐Salicylidene Glycinato Complex for the Selective Fluorometric Detection of Homocysteine over 20 Proteinogenic Amino Acids