The Isospin Distribution of Fragments in Reactions 96Ru+96Ru, 96Ru+96Zr, 96Zr+96Ru, and 96Zr+96Zr at Beam Energy 400 AMeV

The isospin distribution of particles and fragments in collisions 96Ru+96Ru, 96Ru+96Zr, 96Zr+96Ru, and 96Zr+96Zr at beam energy 400 AMeV is studied with isospin dependent QMD model. We find that the rapidity distribution of differential neutron-proton counting in neutron rich nucleus-nucleus collisions at intermediate energies is sensitive to the isospin dependent part of nuclear potential. The study of the N/Z ratio of nucleons, light charged particles (LCP) and intermediate mass fragments (IMF) shows that the isospin dependent part of nuclear potential drives IMF to be more isospin symmetric and emitted nucleons to be more neutron rich. From the study of the time evolution of the isospin distribution in emitted nucleons, LCP and IMF we find that neutrons diffuse much faster than protons at beginning and the final isospin distribution is a result of dynamical balance of symmetry potential and Coulomb force under the charge conservation.Comment: 10 pages, 5 figure

Inhibiting parasite proliferation using a rationally designed anti-tubulin agent

Infectious diseases caused by apicomplexan parasites remain a global public health threat. The presence of multiple ligand-binding sites in tubulin makes this protein an attractive target for anti-parasite drug discovery. However, despite remarkable successes as anti-cancer agents, the rational development of protozoan parasite-specific tubulin drugs has been hindered by a lack of structural and biochemical information on protozoan tubulins. Here, we present atomic structures for a protozoan tubulin and microtubule and delineate the architectures of apicomplexan tubulin drug-binding sites. Based on this information, we rationally designed the parasite-specific tubulin inhibitor parabulin and show that it inhibits growth of parasites while displaying no effects on human cells. Our work presents for the first time the rational design of a species-specific tubulin drug providing a framework to exploit structural differences between human and protozoa tubulin variants enabling the development of much-needed, novel parasite inhibitors. Natacha *#1, Ashwani *#1, Izra , Tianyang **3, Fiona **3, Alexander D. , Valentin , Mamata , Anthony J. , Carolyn A. , Naomi & Michel O.