Journal of medicinal chemistry
Histone deacetylase inhibitors (HDACi) are established anticancer drugs, especially in hematological cancers. This study aimed to design, synthesize, and evaluate a set of HDACi featuring a pentyloxyamide connecting unit linker region and substituted phenylthiazole cap groups. A structural optimization program yielded HDACi with nanomolar inhibitory activity against histone deacetylase class I/IIb enzymes. The novel inhibitors ( and ) showed superior antileukemic activity compared to several approved HDACi. Furthermore, and displayed synergistic activity when combined with chemotherapeutics, decitabine, and clofarabine. In vitro pharmacokinetic studies showed the most promising profile for with intermediate microsomal stability, excellent plasma stability, and concentration-independent plasma protein binding. Additionally, demonstrated comparable in vivo pharmacokinetics to vorinostat. When administered in vivo, effectively inhibited the proliferation of leukemia cells without causing toxicity. Furthermore, the binding modes of and to the catalytic domain 2 of HDAC6 from were determined by X-ray crystallography.
PMID: 39602240