Show simple item record

dc.contributor.authorRathnayake, Athri D.
dc.contributor.authorKim, Yunjeong
dc.contributor.authorDampalla, Chamandi S.
dc.contributor.authorNguyen, Harry Nhat
dc.contributor.authorJesri, Abdul Rahman M.
dc.contributor.authorKashipathy, Maithri M.
dc.contributor.authorLushington, Gerald Henry
dc.contributor.authorBattaile, Kevin P.
dc.contributor.authorLovell, Scott
dc.contributor.authorChang, Kyeong-Ok
dc.contributor.authorGroutas, William C.
dc.identifier.citationAthri D. Rathnayake, Yunjeong Kim, Chamandi S. Dampalla, Harry Nhat Nguyen, Abdul-Rahman M. Jesri, Maithri M. Kashipathy, Gerald H. Lushington, Kevin P. Battaile, Scott Lovell, Kyeong-Ok Chang, and William C. Groutas. Structure-Guided Optimization of Dipeptidyl Inhibitors of Norovirus 3CL Protease. Journal of Medicinal Chemistry 2020 63 (20), 11945-11963en_US
dc.descriptionClick on the DOI link to access the article (may not be free).en_US
dc.description.abstractAcute gastroenteritis caused by noroviruses has a major impact on public health worldwide in terms of morbidity, mortality, and economic burden. The disease impacts most severely immunocompromised patients, the elderly, and children. The current lack of approved vaccines and small-molecule therapeutics for the treatment and prophylaxis of norovirus infections underscores the need for the development of norovirus-specific drugs. The studies described herein entail the use of the gem-dimethyl moiety as a means of improving the pharmacological activity and physicochemical properties of a dipeptidyl series of transition state inhibitors of norovirus 3CL protease, an enzyme essential for viral replication. Several compounds were found to be potent inhibitors of the enzyme in biochemical and cell-based assays. The pharmacological activity and cellular permeability of the inhibitors were found to be sensitive to the location of the gem-dimethyl group.en_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofseriesJournal of Medicinal Chemistry;v.63:no.20
dc.subjectInfectious diseasesen_US
dc.subjectPeptides and proteinsen_US
dc.subjectOrganic compoundsen_US
dc.titleStructure-guided optimization of dipeptidyl inhibitors of Norovirus 3CL proteaseen_US
dc.rights.holder© 2020 American Chemical Societyen_US

Files in this item


There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record