{"database":"biostudies-other","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["3(6)"],"submitter":["Song J"],"journal":["ACS medicinal chemistry letters"],"pagination":["450-3"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4025852"],"abstract":["A series of 36 thiosemicarbazone analogues containing the thiochromanone molecular scaffold functionalized primarily at the C-6 position were prepared by chemical synthesis and evaluated as inhibitors of cathepsins L and B. The most promising inhibitors from this group are selective for cathepsin L and demonstrate IC50 values in the low nanomolar range. In nearly all cases, the thiochromanone sulfide analogues show superior inhibition of cathepsin L as compared to their corresponding thiochromanone sulfone derivatives. Without exception, the compounds evaluated were inactive (IC50 > 10000 nM) against cathepsin B. The most potent inhibitor (IC50 = 46 nM) of cathepsin L proved to be the 6,7-difluoro analogue 4. This small library of compounds significantly expands the structure-activity relationship known for small molecule, nonpeptidic inhibitors of cathepsin L."],"repository":["biostudies-other"],"pmcid":["PMC4025852"],"data_source":["Europe PMC"],"pubmed_authors":["Bayeh L","Conner ES","Chavarria GE","Charlton-Sevcik AK","Kumar GD","Pinney KG","Jones LM","Trawick ML","Song J","Chaplin DJ","Chen SE"],"additional_accession":[]},"is_claimable":false,"name":"Synthesis and biochemical evaluation of thiochromanone thiosemicarbazone analogues as inhibitors of cathepsin L.","description":"A series of 36 thiosemicarbazone analogues containing the thiochromanone molecular scaffold functionalized primarily at the C-6 position were prepared by chemical synthesis and evaluated as inhibitors of cathepsins L and B. The most promising inhibitors from this group are selective for cathepsin L and demonstrate IC50 values in the low nanomolar range. In nearly all cases, the thiochromanone sulfide analogues show superior inhibition of cathepsin L as compared to their corresponding thiochromanone sulfone derivatives. Without exception, the compounds evaluated were inactive (IC50 > 10000 nM) against cathepsin B. The most potent inhibitor (IC50 = 46 nM) of cathepsin L proved to be the 6,7-difluoro analogue 4. This small library of compounds significantly expands the structure-activity relationship known for small molecule, nonpeptidic inhibitors of cathepsin L.","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Jun","modification":"2019-03-27T01:28:30Z","creation":"2019-03-27T01:28:30Z"},"accession":"S-EPMC4025852","cross_references":{"pubmed":["24900494"],"doi":["10.1021/ml200299g "]}}