7 research outputs found
Quantum control and the Strocchi map
Identifying the real and imaginary parts of wave functions with coordinates
and momenta, quantum evolution may be mapped onto a classical Hamiltonian
system. In addition to the symplectic form, quantum mechanics also has a
positive-definite real inner product which provides a geometrical
interpretation of the measurement process. Together they endow the quantum
Hilbert space with the structure of a K\"{a}ller manifold. Quantum control is
discussed in this setting. Quantum time-evolution corresponds to smooth
Hamiltonian dynamics and measurements to jumps in the phase space. This adds
additional power to quantum control, non unitarily controllable systems
becoming controllable by ``measurement plus evolution''. A picture of quantum
evolution as Hamiltonian dynamics in a classical-like phase-space is the
appropriate setting to carry over techniques from classical to quantum control.
This is illustrated by a discussion of optimal control and sliding mode
techniques.Comment: 16 pages Late
Analysis of the Mechanism by Which the Small-Molecule CCR5 Antagonists SCH-351125 and SCH-350581 Inhibit Human Immunodeficiency Virus Type 1 Entry
Human immunodeficiency virus type 1 (HIV-1) entry is mediated by the consecutive interaction of the envelope glycoprotein gp120 with CD4 and a coreceptor such as CCR5 or CXCR4. The CCR5 coreceptor is used by the most commonly transmitted HIV-1 strains that often persist throughout the course of infection. Compounds targeting CCR5-mediated entry are a novel class of drugs being developed to treat HIV-1 infection. In this study, we have identified the mechanism of action of two inhibitors of CCR5 function, SCH-350581 (AD101) and SCH-351125 (SCH-C). AD101 is more potent than SCH-C at inhibiting HIV-1 replication in primary lymphocytes, as well as viral entry and gp120 binding to cell lines. Both molecules also block the binding of several anti-CCR5 monoclonal antibodies that recognize epitopes in the second extracellular loop of CCR5. Alanine mutagenesis of the transmembrane domain of CCR5 suggests that AD101 and SCH-C bind to overlapping but nonidentical sites within a putative ligand-binding cavity formed by transmembrane helices 1, 2, 3, and 7. We propose that the binding of small molecules to the transmembrane domain of CCR5 may disrupt the conformation of its extracellular domain, thereby inhibiting ligand binding to CCR5