Messick, Troy E.; Tolvinski, Lois; Zartler, Edward R.; Moberg, Anna; Frostell, Asa; Smith, Garry R.; Reitz, Allen B.; Lieberman, Paul M. published the artcile< Biophysical screens identify fragments that bind to the viral DNA-binding proteins EBNA1 and LANA>, Synthetic Route of 86129-63-7, the main research area is DNA EBNA1 LANA protein ligand interaction binding fragment NMR; biophys screen surface plasmon resonance saturation transfer difference; Epstein–Barr nuclear antigen 1; Epstein–Barr virus; Kaposi’s sarcoma associated herpesvirus (KSHV); fragment-based lead discovery; latency-associated nuclear antigen; protein–DNA interaction; saturation transfer difference-nuclear magnetic resonance; surface plasmon resonance.
The human gamma-herpesviruses Epstein-Barr virus (EBV) (HHV-4) and Kaposi’s sarcoma-associated herpesvirus (KSHV) (HHV-8) are responsible for a number of diseases, including various types of cancer. Epstein-Barr nuclear antigen 1 (EBNA1) from EBV and latency-associated nuclear antigen (LANA) from KSHV are viral-encoded DNA-binding proteins that are essential for the replication and maintenance of their resp. viral genomes during latent, oncogenic infection. As such, EBNA1 and LANA are attractive targets for the development of small-mol. inhibitors. To this end, we performed a biophys. screen of EBNA1 and LANA using a fragment library by saturation transfer difference (STD)-NMR spectroscopy and surface plasmon resonance (SPR). We identified and validated a number of unique fragment hits that bind to EBNA1 or LANA. We also determined the high-resolution crystal structure of one fragment bound to EBNA1. Results from this screening cascade provide new chem. starting points for the further development of potent inhibitors for this class of viral proteins.
Molecules published new progress about Affinity. 86129-63-7 belongs to class pyridine-derivatives, and the molecular formula is C9H9Cl2NO2, Synthetic Route of 86129-63-7.