ASU Electronic Theses and Dissertations
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Cyanovirin-N (CVN) is a cyanobacterial lectin with potent anti-HIV activity, mediated by binding to the N-linked oligosaccharide moiety of the envelope protein gp120. CVN offers a scaffold to develop multivalent carbohydrate-binding proteins with tunable specificities and affinities. I present here biophysical calculations completed on a monomeric-stabilized mutant of cyanovirin-N, P51G-m4-CVN, in which domain A binding activity is abolished by four mutations; with comparisons made to CVN<super>mutDB</super>, in which domain B binding activity is abolished. Using Monte Carlo calculations and docking simulations, mutations in CVN<super>mutDB</super> were considered singularly, and the mutations E41A/G and T57A were found to impact the affinity towards …
- Woodrum, Brian William, Ghirlanda, Giovanna, Redding, Kevin, et al.
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