Chelator Fragment Library from OTAVA
Résumé
Approximately half of all proteins contain metal ions in the active site for their biological activity. Metalloproteins are involved in many different cellular functions, such as storage and transport of proteins, enzymes and signal transduction proteins. A number of metalloproteins are associated with diseases ranging from pathogenic infections to cancer and therefore have been considered to be promising targets for drug discovery. Fragment-based lead design (FBLD) is an important strategy for the identification of metalloenzyme inhibitors. Chelators demonstrate binding affinities suitable for FBLD screening and provide a diverse range of molecular platforms which can be used for developing lead compounds. Also, the propensity for chelators to bind metal ions allows better prediction of their probable binding position within a protein active site in the absence of experimental structural data of the complex. OTAVA Ltd. offers new Chelator Fragment Library that comprises 575 compounds. The assembled library contains compounds with chelating groups only. Molecular weight of compounds is less than 300 Da. ClogP, number of rotatable bonds and number of H donors are ≤ 3, number of H acceptors and sum of halogen atoms are ≤ 4. The LogSw values are less than -5, PSA is less than 80. All compounds have at least one ring. This library provides an excellent basis for development of metalloprotein inhibitors. More information about this library you can find at www.otavachemicals.com.