Implementing Health Sciences After-School Programming for Mississippi High School Students: the Impact of Social Determinants of Health

Corresponding author (Pharmacy Administration): Saara Nasruddin, [email protected]://egrove.olemiss.edu/pharm_annual_posters_2022/1013/thumbnail.jp

Inspiring Minds, Exploring Science with Project SCORE Curriculum

Corresponding author (Pharmacy Administration): Tess Johnson, [email protected]://egrove.olemiss.edu/pharm_annual_posters_2022/1009/thumbnail.jp

Health Matters: Student-Developed Research Questions by Project SCORE Students

Corresponding author (Health, Exercise Science, and Recreation Management): Melissa Presley, [email protected]://egrove.olemiss.edu/pharm_annual_posters_2022/1015/thumbnail.jp

A diverse view of science to catalyse change

Valuing diversity leads to scientific excellence, the progress of science and, most importantly, it is simply the right thing to do. We must value diversity not only in words, but also in actions

A diverse view of science to catalyse change:Valuing diversity leads to scientific excellence, the progress of science and, most importantly, it is simply the right thing to do. we must value diversity not only in words, but also in actions

No abstract available.publishe

Topoisomerase II-Drug Interaction Domains: Identification of Substituents on Etoposide that Interact with the Enzyme

Etoposide is one of the most successful chemotherapeutic agents used for the treatment of human cancers. The drug kills cells by inhibiting the ability of topoisomerase II to ligate nucleic acids that it cleaves during the double-stranded DNA passage reaction. Etoposide is composed of a polycyclic ring system (rings A–D), a glycosidic moiety at the C4 position, and a pendant ring (E–ring) at the C1 position. Although drug-enzyme contacts, as opposed to drug-DNA interactions, mediate the entry of etoposide into the topoisomerase II-drug-DNA complex, the substituents on etoposide that interact with the enzyme have not been identified. Therefore, saturation transfer difference [1H]- nuclear magnetic resonance spectroscopy and protein-drug competition binding assays were employed to define the groups on etoposide that associate with yeast topoisomerase II and human topoisomerase IIα. Results indicate that the geminal protons of the A–ring, the H5 and H8 protons of the B–ring, as well as the H2’ and H6’ protons and the 3’– and 5’–methoxyl protons of the pendent E–ring interact with both enzymes in the binary protein-ligand complexes. In contrast, no significant nuclear Overhauser enhancement signals arising from the C–ring, the D–ring, or the C4 glycosidic moiety were observed with either enzyme, suggesting that there is limited or no contact between these portions of etoposide and topoisomerase II in the binary complex. The functional importance of E–ring substituents was confirmed by topoisomerase II-mediated DNA cleavage assays