Analysis of Strong-Coupling Parameters for Superfluid 3He

Superfluid $^{3}$He experiments show strong deviation from the weak-coupling limit of the Ginzburg-Landau theory, and this discrepancy grows with increasing pressure. Strong-coupling contributions to the quasiparticle interactions are known to account for this effect and they are manifest in the five $\beta$-coefficients of the fourth order Ginzburg-Landau free energy terms. The Ginzburg-Landau free energy also has a coefficient $g_{z}$ to include magnetic field coupling to the order parameter. From NMR susceptibility experiments, we find the deviation of $g_{z}$ from its weak-coupling value to be negligible at all pressures. New results for the pressure dependence of four different combinations of $\beta$-coefficients, $\beta$_{345}, $\beta$_{12}, $\beta$_{245}, and $\beta$_{5} are calculated and comparison is made with theory.Comment: 6 pages, 2 figures, 1 table. Manuscript prepared for QFS200

Polyamine-containing etoposide derivatives as poisons of human type II topoisomerases: Differential effects on topoisomerase II\u3b1 and II\u3b2

Etoposide is an anticancer drug that acts by inducing topoisomerase II-mediated DNA cleavage. Despite its wide use, etoposide is associated with some very serious side-effects including the development of treatment-related acute myelogenous leukemias. Etoposide targets both human topoisomerase II alpha and II beta. However, the contributions of the two enzyme isoforms to the therapeutic vs. leukemogenic properties of the drug are unclear. In order to develop an etoposide-based drug with specificity for cancer cells that express an active polyamine transport system, the sugar moiety of the drug has been replaced with a polyamine tail. To analyze the effects of this substitution on the specificity of hybrid molecules toward the two enzyme isoforms, we analyzed the activity of a series of etoposide-polyamine hybrids toward human topoisomerase II alpha and II beta. All of the compounds displayed an ability to induce enzyme-mediated DNA cleavage that was comparable to or higher than that of etoposide. Relative to the parent drug, the hybrid compounds displayed substantially higher activity toward topoisomerase II beta than II alpha. Modeling studies suggest that the enhanced specificity may result from interactions with Gln778 in topoisomerase II beta. The corresponding residue in the a isoform is a methionine