Meyer-Almes - Molecular determinants
Determinants of molecular recognition between ligands and HDACs.
Although enzymes of the histone deacetylase (HDAC) family exhibit a highly conserved binding sites, similar ligand structures are shown to have dramatic differences on both, affinity and selectivity. The underlying forces are investigated using a combined approach of site directed mutagenesis, biochemical and biophysical methods. Further information can be found on these posters:kinetics1 and kinetics2.
Publications
C.E. Weston, A. Krämer, F. Colin, Ö. Yildiz, M.G.J. Baud, F.-J. Meyer-Almes, M. Fuchter, Toward photopharmacological antimicrobial chemotherapy using photoswitchable amidohydrolase inhibitors, ACS Infect. Dis. (2016), DOI: 10.1021/acsinfecdis.6b00148.
F.-J. Meyer-Almes, Discrimination between conformational selection and induced fit protein-ligand binding using integrated global fit analysis, Eur. Biophys. J. (2016) 45, 245-257.
F.-J. Meyer-Almes, Kinetic binding assays for the analysis of protein-ligand interactions, Drug Discovery Today: Technologies (2015) 17, 1-8.
C. Meyners, M.G. Baud, M.J. Fuchter, F.-J. Meyer-Almes, Kinetic method for the large-scale analysis of the binding mechanism of histone deacetylase inhibitors, Anal. Biochem. 460, 39-46 (2014).
C. Meyners, M.G. Baud, M.J. Fuchter, F.-J. Meyer-Almes, Thermodynamics of ligand binding to histone deacetylase like amidohydrolase from Bordetella/Alcaligenes, J. Mol. Recognit. 27, 160-72 (2014).