Address: Room 43, 2nd Floor, New Building, School of Pharmacy, University of Ghana Legon
Tel: 0208260595
Email: kfopuni@ug.edu.gh
ORCID: https://orcid.org/my-orcid?orcid=0000-0003-1653-1458
Scopus ID: https://www.scopus.com/authid/detail.uri?authorId=57205293494
PubMed: https://pubmed.ncbi.nlm.nih.gov/?term=opuni%20kf
Research Gate: https://www.researchgate.net/profile/Kwabena-Opuni-2
Google Scholar: https://scholar.google.com/citations?user=KLNLXHAAAAAJ&hl=en&oi=ao
This research work focused on developing electrospray mass spectrometry-based epitope mapping methods in the gas phase. Intact Transition Epitope Mapping – One-step Non-covalent force Exploitation (ITEM-ONE), a mass spectrometric epitope mapping method in which epitopes are identified by the accurate masses of the complex released peptides, was developed. Also, the Intact Transition Epitope Mapping – Targeted High-Energy Rupture of Extracted Epitopes (ITEM-THREE) method identifies epitope peptides by partial amino acid sequencing of the CoRPs rapidly and accurately. In both methods, neither antibodies nor immune complexes are immobilized. Instead, both methods used ion mobility mass spectrometry for ion separation coupled with gas phase dissociation of immune complexes in the mass spectrometer's collision cell. The speed by which ITEM-ONE or ITEM-THREE can be conducted and the low required sample amounts outperform many of the other epitope mapping methods. Intact Transition Epitope Mapping - Thermodynamic Weak-force Order (ITEM-TWO) enables rapid epitope mapping and determination of apparent dissociation energies of immune complexes with minimal in-solution handling and characterizes two most important antibody properties, specificity, and affinity has been developed. ITEM-TWO was used to investigate the influence of a solvent’s composition on the stability of desorbed and multiply charged RNAse S ions by analyzing the non-covalent complex’s gas-phase dissociation processes. From the experimental data, it is concluded that the stability of RNAse S in the gas phase is independent of its in-solution equilibrium but is sensitive to the complexes’ gas-phase charge states. Bio-computational in-silico studies explained quantitative experimental data with single amino acid residue resolution.
This research focused on the mass spectrometric characterization of the MSP119 antigen to antiMSP119 (G17.12) monoclonal antibody interaction. The malarial antigen-containing fusion protein, MBP-pfMSP119, was cloned in Escherichia coli, which was structurally and functionally characterized before and after high pressure–assisted enzymatic digestion. ITEM-THREE was used to determine the area on the MBP-pfMSP119 antigen surface recognized by the antipfMSP119 antibody G17.12, which was part of an assembled epitope on the MBP-pfMSP119 antigen. This research established a workflow to obtain high quality control data for diagnostic assays, including ITEM-THREE as a powerful analytical tool. Further studies are being conducted on the computational design of MSP119 malaria antigen mimotope peptide and mass spectrometric characterization of molecular details of the predicted mimotope peptide as well as mass spectrometric investigations of antibody complexes to gain experimental details of specificity and affinity. Commercially available antibody for the detection of MSP119-specific malaria antigen in patients’ sera by ELISA will then be applied. Finally, developing the MSP119 malaria antigen mimotope peptide as a screening assay to determine the presence of anti-malaria antibody titers in persons who have gained immuno-protection either via vaccination or naturally will be conducted.
The goal of this study was to use combined screening methods for the rapid detection of substandard/falsified medicines since it has become a global public health challenge. This study used three screening methods (GPHF Minilab, Colorimetry, and Counterfeit Drug Indicator) and one confirmatory method (high-performance liquid chromatography) for the quality assessment of different batches of artemether/lumefantrine dosage forms. The study's outcome showed that the combined screening methods and the confirmatory method provided equivalent quality assessment profiles and therefore demonstrated the usefulness of combined screening methods for the detection of falsified and/or substandard medicines in the absence of a confirmatory method. This approach is cheap, rapid, and can be applied to field monitoring substandard/falsified medicines.
Studies undertaken in this area assessed the quality of herbal medicinal products. These studies focused on a) the determination of residual solvents in herbal medicinal products using gas chromatography, b) monitoring and risk assessment of pesticide residues in herbal medicinal products using gas chromatography-mass spectrometry, c) classification of herbal medicinal products using XRF spectroscopy in combination with chemometric analysis, and d) classification and detection of expired antimalarial herbal medicinal product using ultraviolet-visible spectroscopy and chemometrics. These studies documented the presence of residual solvents and pesticide residues in some herbal medicinal products in Ghana. Also, these studies showed that analytical methods combined with a chemometric strategy could be used for a) the classification and detection of antimalarial herbal medicinal products and b) the classification of herbal medicinal products into various therapeutic agents based on their elemental composition. These studies suggested the need for continual monitoring of contaminants in herbal medicinal products as a public health concern and the potential need for more stringent regulation of herbal medicinal products marketed in Ghana.
This research focused on applying analytical methods for pharmacokinetics studies of drugs and drug-drug interaction. This work focused on the pharmacokinetics of drugs using animal models. The studies documented the effect of a) betamethasone on the pharmacokinetics of amikacin, b) aminophylline on the pharmacokinetics of amikacin, and c) the effect of Cellgevity® on the pharmacokinetics of carbamazepine. Results from the studies showed a) the possible interaction between aminophylline and amikacin, b) betamethasone altered the pharmacokinetics of amikacin, and c) Cellgevity® altered the pharmacokinetics of carbamazepine.
Education
Mar 2017 Doctor of Philosophy (PhD) (Summa cum laude), Proteome Center Rostock, Institute of Immunology, University of Rostock, Rostock, Germany.
Dec 2004 Master of Pharmaceutical Analysis and Quality Control (MSc), Faculty of Pharmacy and Pharmaceutical Sciences, Kwame Nkrumah University of Science and Technology, Kumasi, Ghana.
Mar 2002 Certificate in Management of Drug Supplies (Cert), Robert Gordon University, Scotland.
Jul 2001 Bachelor of Pharmacy (B. Pharm), Faculty of Pharmacy and Pharmaceutical Sciences, Kwame Nkrumah University of Science and Technology, Kumasi, Ghana.
May-Jul 2019 Post-Doctoral Fellow, Proteome Center Rostock, Institute of Immunology, University of Rostock, Rostock, Germany.
Feb 2022 Associate Professor, Department of Pharmaceutical Chemistry, School of Pharmacy, University of Ghana, Accra, Ghana.
July 2017 Senior Lecturer, Department of Pharmaceutical Chemistry, School of Pharmacy, University of Ghana, Accra, Ghana.
Mar 2017 Lecturer, Department of Pharmaceutical Chemistry, School of Pharmacy, University of Ghana, Accra, Ghana.
Aug 2010 Assistant Lecturer, Department of Pharmaceutical Chemistry, School of Pharmacy, University of Ghana, Accra, Ghana.
Aug 2021 to date Coordinator, PharmD Top Up Programme, School of Pharmacy, University of Ghana, Accra, Ghana.
2020 - 2022 Head, Department of Pharmaceutical Chemistry, School of Pharmacy, University of Ghana, Accra, Ghana.
10-14 Feb 2020 Acting Dean, School of Pharmacy, University of Ghana, Accra, Ghana.
2018 - 2020 Acting Head, Department of Pharmaceutical Chemistry, School of Pharmacy, University of Ghana, Accra, Ghana.
2016 - 2018 Coordinator, Seminar and Students Project, School of Pharmacy, University of Ghana, Accra, Ghana.
https://doi.org/10.1007/978-3-031-12398-6_2
https://doi.org/10.1007/978-3-031-12398-6_10
https://doi.org/10.3390/medicina58020226
https://doi.org/10.1155/2022/4625954
https://doi.org/10.5599/admet.1183
https://doi.org/10.1016/j.pmedr.2021.101633
https://doi.org/10.3390/ijms221910183
https://doi.org/10.1155/2021/5592217
https://doi.org/10.1007/s10661-021-09261-1
https://doi.org/10.1016/j.sciaf.2021.e00825
https://doi.org/10.1016/j.jchromb.2021.122750
https://doi.org/10.1111/tmi.13541
https://doi:10.3390/molecules25204776
https://doi.org/10.1155/2020/7956493
https://doi.org/10.1016/j.jprot.2019.103572
https://doi.org/10.1186/s12936-019-3045-y
https://doi.org/10.1016/j.lwt.2022.113498
https://doi.org/10.1074/mcp.RA119.001429
http://dx.doi.org/10.5599/admet.613
https://doi.org/10.1007/s00216-017-0603-4
https://doi.org/10.1177/1469066717722256
https://doi.org/10.1007/s13361-017-1654-7
https://doi.org/10.4172/jpb.1000425
https://doi.org/10.1002/mas.21516
https://doi.org/10.1021/acs.analchem.5b03536
https://doi.org/10.1007/s13361-014-1053-2
https://doi.org/10.1002/jmr.2375
https://dx.doi.org/10.1021/ac402559m