6533b82bfe1ef96bd128cd53
RESEARCH PRODUCT
Tuning and Predicting Biological Affinity: Aryl Nitriles as Cysteine Protease Inhibitors
Cornelia HeindlVeronika EhmkeMatthias RottmannMatthias RottmannFrançois DiederichJose Enrico Q. QuinsaatTanja SchirmeisterTanja SchirmeisterCéline FreymondCéline FreymondReto BrunReto BrunPablo Rivera-fuentessubject
Models MolecularProteasesNitrileCathepsin LTrypanosoma brucei bruceiCysteine Proteinase InhibitorsBiochemistryCysteine Proteinase InhibitorsCathepsin Lchemistry.chemical_compoundCatalytic DomainNitrilesHumansOrganic chemistryPhysical and Theoretical ChemistryCathepsinbiologyArylOrganic ChemistryCombinatorial chemistryCysteine proteaseCysteine EndopeptidaseschemistryDrug Designbiology.proteinCysteinedescription
A series of aryl nitrile-based ligands were prepared to investigate the effect of their electrophilicity on the affinity against the cysteine proteases rhodesain and human cathepsin L. Density functional theory calculations provided relative reactivities of the nitriles, enabling prediction of their biological affinity and cytotoxicity and a clear structure-activity relationship.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2012-02-17 | Org. Biomol. Chem. |