Asteroseismology of the Hyades red giant and planet host epsilon Tauri

Asteroseismic analysis of solar-like stars allows us to determine physical parameters such as stellar mass, with a higher precision compared to most other methods. Even in a well-studied cluster such as the Hyades, the masses of the red giant stars are not well known, and previous mass estimates are based on model calculations (isochrones). The four known red giants in the Hyades are assumed to be clump (core-helium-burning) stars based on their positions in colour-magnitude diagrams, however asteroseismology offers an opportunity to test this assumption. Using asteroseismic techniques combined with other methods, we aim to derive physical parameters and the evolutionary stage for the planet hosting star epsilon Tau, which is one of the four red giants located in the Hyades. We analysed time-series data from both ground and space to perform the asteroseismic analysis. By combining high signal-to-noise (S/N) radial-velocity data from the ground-based SONG network with continuous space-based data from the revised Kepler mission K2, we derive and characterize 27 individual oscillation modes for epsilon Tau, along with global oscillation parameters such as the large frequency separation and the ratio between the amplitude of the oscillations measured in radial velocity and intensity as a function of frequency. The latter has been measured previously for only two stars, the Sun and Procyon. Combining the seismic analysis with interferometric and spectroscopic measurements, we derive physical parameters for epsilon Tau, and discuss its evolutionary status.Comment: 13 pages, 13 figures, 4 tables, accepted for publication in Astronomy & Astrophysic

Targeting undruggable carbohydrate recognition sites through focused fragment library design

Carbohydrate-protein interactions are key for cell-cell and host-pathogen recognition and thus, emerged as viable therapeutic targets. However, their hydrophilic nature poses major limitations to the conventional development of drug-like inhibitors. To address this shortcoming, four fragment libraries were screened to identify metal-binding pharmacophores (MBPs) as novel scaffolds for inhibition of Ca2+-dependent carbohydrate-protein interactions. Here, we show the effect of MBPs on the clinically relevant lectins DC-SIGN, Langerin, LecA and LecB. Detailed structural and biochemical investigations revealed the specificity of MBPs for different Ca2+-dependent lectins. Exploring the structure-activity relationships of several fragments uncovered the functional groups in the MBPs suitable for modification to further improve lectin binding and selectivity. Selected inhibitors bound efficiently to DCSIGN-expressing cells. Altogether, the discovery of MBPs as a promising class of Ca2+- dependent lectin inhibitors creates a foundation for fragment-based ligand design for future drug discovery campaigns