Application of bidentate N,N'-donor extractants in the hydrometallurgical separation of base metals from an acidic sulfate medium
- Authors: Okewole, Adeleye Ishola
- Date: 2013
- Subjects: Hydrometallurgy Sulfates Nanofibers Electrospinning Sorbents Extraction (Chemistry) Solvent extraction Stereochemistry
- Language: English
- Type: Thesis , Doctoral , PhD
- Identifier: vital:4281 , http://hdl.handle.net/10962/d1002610
- Description: Bidentate imidazole-based extractants, 1-octylimidazole-2-aldoxime (OIMOX) and 1-octyl-2-(2′-pyridyl)imidazole (OPIM), along with dinonylnaphthalene sulfonic acid (DNNSA) as a synergist, were investigated as potential selective extractants for Cu²⁺and Ni²⁺ respectively from base metals in a solvent extraction system. The study was extended to evaluate the sorption and separation of Ni²⁺ from other base metals in a solid-solution system using microspherical Merrifield resins and nanofibers functionalized with 2,2′-pyridylimidazole. Copper was effectively separated with OIMOX and DNNSA as extractants from nickel with ΔpH½ ≈1.05 and the extraction order of Cu²⁺ > Ni²⁺ > Zn²⁺ > Cd²⁺> Co²⁺ was achieved as a function of pH. At pH 1.65 the extracted copper, from a synthetic mixture of the base metals reached 90.13(±0.90)%, and through a two-step extraction process 98.22(±0.29)% copper was recovered with negligible nickel and cobalt impurities. Stripping of the copper from the loaded organic phase using TraceSelect sulphuric acid at pH 0.35 yielded 96.60(±0.44)% of the loaded quantity after the second stage of stripping. The separation of Ni²⁺ from the borderline and hard acids; Co²⁺, Cu²⁺, Zn²⁺, Fe2²⁺, Fe²⁺, Mn²⁺, Mg2²⁺ and Ca²⁺ at a pH range of 0.5-3.5 with OPIM and DNNSA was acvieved to the tune of a ΔpH½≈ 1.6 with respect to cobalt from a sulfate and sulfate/chloride media. A three-stage counter-current extraction of Ni²⁺, at the optimized pH of 1.89, from a synthetic mixture of Ni²⁺, Co²⁺ and Cu²⁺, yielded 99.01(±1.79)%. The total co-extracted Cu²⁺ was 48.72(±0.24)% of the original quantity in the mixture, and it was 19.85(±0.28%) for Co²⁺. The co-extracted Cu²⁺ was scrubbed off from the loaded organic phase at pH≈8.5 by using an ammonium buffer, while co-extracted Co²⁺ was selectively and quantitatively stripped with H₂SO₄ at pH 1.64. The total recovery of Ni²⁺ by stripping at pH 0.32 was 94.05(±1.70)%. In the solid-liquid system, Ni²⁺ was separated from Co²⁺, Cu²⁺, and Fe²⁺ with the microspherical resins funtionalised with 2,2′-pyridylimidazole by a separation factor (β) in the range 22-45. Electrospun nanofibers as sorbents yielded high sorption capacity in the range of 0.97 - 1.45 mmol.g⁻¹ for the same metals ions. Thus, 1-octylimidazole-2-aldoxime (OIMOX), and1-octyl-2-(2′-pyridyl)imidazole (OPIM) can be effectively utilized alongside DNNSA as a co-extractant in the separation of Cu²⁺ and Ni²⁺ respectively from base metals in acidic sulfate medium in a solvent extraction process, and the latter as a selective ligand in the solid-liquid separation of Ni²⁺ from Co²⁺, Cu²⁺, and Fe²⁺.
- Full Text:
- Date Issued: 2013
In-silico analysis of Plasmodium falciparum Hop protein and its interactions with Hsp70 and Hsp90
- Authors: Clitheroe, Crystal-Leigh
- Date: 2013
- Subjects: Plasmodium falciparum , Heat shock proteins , Molecular chaperones , Homology (Biology) , Protein-protein interactions , Malaria -- Chemotherapy
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:3896 , http://hdl.handle.net/10962/d1003819 , Plasmodium falciparum , Heat shock proteins , Molecular chaperones , Homology (Biology) , Protein-protein interactions , Malaria -- Chemotherapy
- Description: A lessor understood co-chaperone, the Hsp70/Hsp90 organising protein (Hop), has been found to play an important role in modulating the activity and co-interaction of two essential chaperones; Hsp90 and Hsp70. The best understood aspects of Hop so far indicate that residues in the concave surfaces of the three tetratricopeptide repeat (TPR) domains in the protein bind selectively to the C-terminal motifs of Hsp70 and Hsp90. Recent research suggests that P. falciparum Hop (PfHop), PfHsp90 and PfHsp70 do interact and form complex in the P. falciparum trophozooite and are overexpressed in this infective stage. However, there has been almost no computational research on malarial Hop protein in complex with other malarial Hsps.The current work has focussed on several aspects of the in-silico characterisation of PfHop, including an in-depth multiple sequence alignment and phylogenetic analysis of the protein; which showed that Hop is very well conserved across a wide range of available phyla (four Kingdoms, 60 species). Homology modelling was employed to predict several protein structures for these interactions in P. falciparum, as well as predict structures of the relevant TPR domains of Human Hop (HsHop) in complex with its own Hsp90 and Hsp70 C-terminal peptide partners for comparison. Protein complex interaction analyses indicate that concave TPR sites bound to the C-terminal motifs of partner proteins are very similar in both species, due to the excellent conservation of the TPR domain’s “double carboxylate binding clamp”. Motif analysis was combined with phylogenetic trees and structure mapping in novel ways to attain more information on the evolutionary conservation of important structural and functional sites on Hop. Alternative sites of interaction between Hop TPR2 and Hsp90’s M and C domains are distinctly less well conserved between the two species, but still important to complex formation, making this a likely interaction site for selective drug targeting. Binding and interaction energies for all modelled complexes have been calculated; indicating that all HsHop TPR domains have higher affinities for their respective C-terminal partners than do their P. falciparum counterparts. An alternate motif corresponding to the C-terminal motif of PfHsp70-x (exported to the infected erythrocyte cytosol) in complex with both human and malarial TPR1 and TPR2B domains was analysed, and these studies suggest that the human TPR domains have a higher affinity for this motif than do the respective PfHop TPR domains. This may indicate potential for a cross species protein interaction to take place, as PfHop is not transported to the human erythrocyte cytosol.
- Full Text:
- Date Issued: 2013