Ontology highlight
ABSTRACT:
SUBMITTER: Boudreau PD
PROVIDER: S-EPMC7240701 | biostudies-literature | 2019 Oct
REPOSITORIES: biostudies-literature
Journal of medicinal chemistry 20191004 20
Gallinamide A, originally isolated with a modest antimalarial activity, was subsequently reisolated and characterized as a potent, selective, and irreversible inhibitor of the human cysteine protease cathepsin L. Molecular docking identified potential modifications to improve binding, which were synthesized as a suite of analogs. Resultingly, this current study produced the most potent gallinamide analog yet tested against cathepsin L (<b>10</b>, <i>K</i><sub>i</sub> = 0.0937 ± 0.01 nM and <i>k< ...[more]