Vusumuzi Ngonidzashe Hove

@vusumuzihove

Scientific Researcher, Pharmaceutical Sciences and Medicinal Chemistry
University at Buffalo

Vusumuzi Ngonidzashe Hove


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https://researchid.co/vuvuhove
Vusumuzi Ngonidzashe Hove is a medicinal chemistry researcher and pharmaceutical scientist with a focus on clinical oncology. His research involves investigating the therapeutic efficacy, ADME properties, and toxicity of pharmacologic agents (in vitro and in vivo) using pharmacokinetic/pharmacodynamic (PK/PD) modeling. Another aspect of his work includes identifying clinically relevant drug-drug interactions (DDIs) to inform future regulatory studies on drug disposition. Additionally, he has explored the use of oxime ligands for Fe(III) MRI contrast agents and for sensing Fe(III) and Fe(II).

Hove pursued his undergraduate and graduate studies at the University at Buffalo, earning a Bachelor’s degree in Chemistry and two Master of Science degrees in Medicinal Chemistry and Pharmaceutical Sciences. He was awarded the Professor Emeritus Dr. Thomas J. Bardos Scholarship, presented by the University at Buffalo School of Pharmacy and Pharmaceutical Sciences.

EDUCATION

• St. George's College, Harare, Zimbabwe (2003-2008)

• Bachelor’s Degree in Chemistry (Cum Laude with Distinction) (2010-2014), University at Buffalo, Department of Chemistry

• Master of Science (MS) Degree in Medicinal and Pharmaceutical Chemistry (2016-2019), University at Buffalo, Department of Chemistry

• Master of Science (MS) Degree in Pharmaceutical Sciences (2019-2023), The University at Buffalo School of Pharmacy and Pharmaceutical Sciences

• Ph.D. Degree in Pharmaceutical Sciences (2019-present), The University at Buffalo School of Pharmacy and Pharmaceutical Sciences

RESEARCH, TEACHING, or OTHER INTERESTS

Pharmacology, Toxicology and Pharmaceutics, Organic Chemistry, Drug Discovery, General Chemistry
1

Scopus Publications

16

Scholar Citations

1

Scholar h-index

1

Scholar i10-index

Scopus Publications

  • Influence of Tyrosine Kinase Inhibition on Organic Anion Transporting Polypeptide 1B3-Mediated Uptake
    Vusumuzi N. Hove, Kenneth Anderson, Elizabeth R. Hayden, Kyle Z. Pasquariello, Alice A. Gibson, Shichen Shen, Jun Qu, Yan Jin, Jeffrey C. Miecznikowski, Shuiying Hu, Jason A. Sprowl
    Molecular Pharmacology, 2022
    The organic anion transporting polypeptide family member (OATP) 1B3 is a hepatic uptake transporter that has a broad substrate recognition and plays a significant role in regulating elimination of endogenous biomolecules or xenobiotics. OATP1B3 works in tandem with OATP1B1, with which it shares approximately 80% sequence homology and a high degree of substrate overlap. Despite some substrates being recognized solely by OATP1B3, its ability to compensate for loss of OATP1B1-mediated elimination and recognition by regulatory agencies, little is known about OATP1B3 regulatory factors and how they are involved with drug-drug interaction. It was recently discovered that OATP1B1 function is mediated by the activity of a particular tyrosine kinase that is sensitive to a variety of tyrosine kinase inhibitors (TKIs). This study reports that OATP1B3 is similarly regulated, as at least 50% of its activity is reduced by 20 US Food and Drug Administration -approved TKIs. Nilotinib was assessed as the most potent OATP1B3 inhibitor among the investigated TKIs, which can occur at clinically relevant concentrations and acted predominantly through noncompetitive inhibition without impacting membrane expression. Finally, OATP1B3 function was determined to be sensitive to the knockdown of the Lck/Yes novel tyrosine kinase that is sensitive to nilotinib and has been previously implicated in mediating OATP1B1 activity. Collectively, our findings identify tyrosine kinase activity as a major regulator of OATP1B3 function which is sensitive to kinase inhibition. Given that OATP1B1 is similarly regulated, simultaneous disruption of these transporters can have drastic effects on systemic drug concentrations, which would promote adverse events. SIGNIFICANCE STATEMENT The organic anion transporting polypeptide family member (OATP) 1B3 is a facilitator of hepatic drug elimination, although much is unknown of how OATP1B3 activity is mediated, or how such regulators contribute to drug-drug interactions. This study reports that OATP1B3 activity is dependent on the Lck/Yes novel tyrosine kinase, which is sensitive to numerous tyrosine kinase inhibitors. These findings provide insight into the occurrence of many clinical drug-drug interactions, and a rationale for future study of tyrosine kinases regulating drug disposition.

RECENT SCHOLAR PUBLICATIONS

  • Influence of tyrosine kinase inhibition on organic anion transporting polypeptide 1B3-mediated uptake
    VN Hove, K Anderson, ER Hayden, KZ Pasquariello, AA Gibson, S Shen, ...
    Molecular pharmacology 101 (6), 381-389 , 2022
    2022
    Citations: 16
  • Oxime ligands for Fe (III) MRI contrast agents and for sensing Fe (III) and Fe (II)
    VN Hove
    State University of New York at Buffalo , 2019
    2019

MOST CITED SCHOLAR PUBLICATIONS

  • Influence of tyrosine kinase inhibition on organic anion transporting polypeptide 1B3-mediated uptake
    VN Hove, K Anderson, ER Hayden, KZ Pasquariello, AA Gibson, S Shen, ...
    Molecular pharmacology 101 (6), 381-389 , 2022
    2022
    Citations: 16
  • Oxime ligands for Fe (III) MRI contrast agents and for sensing Fe (III) and Fe (II)
    VN Hove
    State University of New York at Buffalo , 2019
    2019