Calorimetric studies of ternary complexes of Ni(II) and Cu(II) nitrilotriacetic acid and N-acetyloligohistidines

Mehlenbacher, Matthew R.; Bou-Abdallah, Fadi; Liu, Xing Xin; Melman, Artem

doi:10.1016/j.ica.2015.08.009

Cited by 13 publications

(7 citation statements)

References 73 publications

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“…The MS studies began with the characterization of the starting Ac-His-6 22 sample by MALDI-TOF and ESI-TOF in positive-ion mode, and the corresponding spectra are displayed in Fig. 3 .…”

Section: Resultsmentioning

confidence: 99%

“…The polymeric material AcHis-6-MBHA-1d was extracted with chloroform, puried by ash chromatography, and characterized by mass spectrometry (MS) and NMR spectroscopy techniques. The MS studies began with the characterization of the starting Ac-His-6 22 sample by MALDI-TOF and ESI-TOF in positive-ion mode, and the corresponding spectra are displayed in Fig. 3.…”

Section: Synthesismentioning

confidence: 99%

“…22 The synthesis of linear AcHis-6 was performed according to the solid phase approach using standard Fmoc methodology in a CEM Liberty automated microwave peptide synthesizer. N a -Fmoc-N (im) -trityl-L-histidine, Wang-resin supported N a -Fmoc-N (im) -trityl-L-histidine and HBTU were purchased from Chem-Impex International (Illinois, USA).…”

Section: Methyl 2-[hydroxyl[6-(prop-2-ynyloxy)naphthalen-2-yl] Methylmentioning

confidence: 99%

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Poly-histidine grafting leading to fishbone-like architectures

et al. 2018

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A small series of Morita-Baylis-Hillman adduct (MBHA) derivatives was synthesized and made to react with imidazole, N-acetylhistidine, and N-acetylhexahistidine as models of poly-histidine derivatives. Intriguingly, the reaction of MBHA derivatives 1a and b with imidazole in acetonitrile-phosphate buffered saline (PBS) gave the imidazolium salt biadducts 3a and b as the main reaction products. These results were confirmed by experiments performed with N-acetylhistidine and 1b and suggested the possible occurrence of these structures in the products of poly-histidine labeling with MBHA derivatives 1a and b.These compounds were then transformed into the corresponding water-soluble derivatives 1c-e by introducing oligo(ethylene glycol) chains and their reactivity was evaluated in preliminary experiments with imidazole and then with N-acetylhexahistidine in PBS. The structure of polymeric materials Ac-His-6-MBHA-1d and Ac-His-6-MBHA-1e obtained using ten-fold excesses of compounds 1d and e was investigated using mass spectrometry, NMR spectroscopy, and photophysical studies, which suggested the presence of biadduct residues in both polymeric materials. These results provide the basis for the preparation of fishbone-like polymer brushes, the characterization of their properties, and the exploration of their potential applications in different fields of science such as in vivo fluorogenic labeling, fluorescence microscopy, protein PEGylation, up to the production of smart materials and biosensors.

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“…The MS studies began with the characterization of the starting Ac-His-6 22 sample by MALDI-TOF and ESI-TOF in positive-ion mode, and the corresponding spectra are displayed in Fig. 3 .…”

Section: Resultsmentioning

confidence: 99%

Section: Synthesismentioning

confidence: 99%

Section: Methyl 2-[hydroxyl[6-(prop-2-ynyloxy)naphthalen-2-yl] Methylmentioning

confidence: 99%

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Poly-histidine grafting leading to fishbone-like architectures

et al. 2018

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“…This synthesis requires stoichiometric addition of Cu(II)-SO 4 to NTA, but under very specific pH conditions. [45] A step-by-step description of the synthesis can be found in a previously published protocol. [46] Once Cu(II)-NTA is synthesized, protein containing dHis is readily labeled by the stoichiometric addition for Cu(II)-NTA to dHis, even in the 4C).…”

Section: Protein Dynamics With Cu(ii) Labelingmentioning

confidence: 99%

Measurement of Protein Dynamics from Site Directed Cu(II) Labeling

et al. 2022

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This review describes the use of Electron Paramagnetic Resonance (EPR) to measure residue specific dynamics in proteins with a specific focus on Cu(II)-based spin labels. First, we outline approaches used to measure protein motion by nitroxide-based spin labels. Here, we describe conceptual details and outline challenges that limit the use of nitroxide spin labels to solvent-exposed α-helical sites. The bulk of this review showcases the use of newly developed Cu(II)-based protein labels. In this approach, the strategic mutation of native residues on a protein to generate two neighboring Histidine residues (i.e., the dHis motif) is exploited to enable a rigid site-selective binding of a Cu(II) complex. The chelation of the Cu(II) complex to dHis directly anchors the Cu(II) spin label to the protein backbone. The improvement in rigidity expands both the spin-labeling toolkit as well as the resolution of many EPR measurements. We describe how EPR measurements of the Cu(II) label directly reflect backbone motion and fluctuations. The EPR are complemented by Molecular Dynamics simulations. Finally, the dHis motif provides access to the measurement of site-specific dynamics at both α-helices and β-sheets. The review outlines the limitations of the dHis method and provides an outlook for future developments.

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“…This sequence is commonly used for protein isolation via affinity chromatography because of its strong interaction with metal ions, e.g., Ni(II), Co(II), or Cu(II) ( Bornhorst and Falke, 2000 ; Blankespoor et al, 2005 ). For example, the binding of N-acetyl hexahistidine to Cu(II)-nitrilotriacetic acid (NTA) and to Ni(II)-NTA were shown to have dissociation constants of 27.1 and 69.4 µM, respectively ( Mehlenbacher et al, 2015 ).…”

Section: Introductionmentioning

confidence: 99%

A Novel Copper-Binding Peptide That Self-Assembles Into a Transparent Antibacterial and Antiviral Coating

Boas

Reches

2021

Front. Bioeng. Biotechnol.

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The health, economy, and quality of life all over the world are greatly affected by bacterial infections and viral outbreaks. Bacterial cells and viruses, such as influenza, can spread through contaminated surfaces and fomites. Therefore, a possible way to fight these pathogens is to utilize antibacterial and antiviral coatings, which reduce their numbers on contaminated surfaces. Here, we present a novel short peptide that can self-assemble, adhere to various surfaces, and bind different metal ions such as copper, which provides the surface with antibacterial and antiviral properties. For these functions, the peptide incorporates the amino acid 3,4-dihydroxyphenylalanine (DOPA), which provides the peptide with adhesive capabilities; a diphenylalanine motif that induces the self-assembly of the peptide; the metal-binding hexahistidine sequence. Our results demonstrate that the coating, which releases monovalent cuprous ions and hydrogen peroxide, provides the surfaces with significant antibacterial and antiviral properties. Additionally, the coating remains transparent, which is favorable for many objects and especially for display screens.

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Calorimetric studies of ternary complexes of Ni(II) and Cu(II) nitrilotriacetic acid and N-acetyloligohistidines

Cited by 13 publications

References 73 publications

Poly-histidine grafting leading to fishbone-like architectures

Poly-histidine grafting leading to fishbone-like architectures

Measurement of Protein Dynamics from Site Directed Cu(II) Labeling

A Novel Copper-Binding Peptide That Self-Assembles Into a Transparent Antibacterial and Antiviral Coating

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