19146-51-1Relevant articles and documents
Structure-activity relationship studies of dipeptide-based hepsin inhibitors with Arg bioisosteres
Kwon, Hongmok,Ha, Hyunsoo,Jeon, Hayoung,Jang, Jaebong,Son, Sang-Hyun,Lee, Kiho,Park, Song-Kyu,Byun, Youngjoo
supporting information, (2020/12/25)
Hepsin is a type II transmembrane serine protease (TTSP) associated with cell proliferation and overexpressed in several types of cancer including prostate cancer (PCa). Because of its significant role in cancer progression and metastasis, hepsin is an attractive protein as a potential therapeutic and diagnostic biomarker for PCa. Based on the reported Leu-Arg dipeptide-based hepsin inhibitors, we performed structural modification and determined in vitro hepsin- and matriptase-inhibitory activities. Comprehensive structure-activity relationship studies identified that the p-guanidinophenylalanine-based dipeptide analog 22a exhibited a strong hepsin-inhibitory activity (Ki = 50.5 nM) and 22-fold hepsin selectivity over matriptase. Compound 22a could be a prototype molecule for structural optimization of dipeptide-based hepsin inhibitors.
ENANTIOSELECTIVE HYDROLYSIS BY BAKER'S YEAST - II. ESTERS OF N-ACETYL AMINO ACIDS
Glaenzer, B. I.,Faber, K.,Griengl, H.
, p. 771 - 778 (2007/10/02)
D-N-Acetyl amino acid esters were obtained via enantioselective hydrolysis of their racemates by use of fermenting yeast.Evidence is given that proteinases are the enzymes involved.
ENANTIOSELECTIVE HYDROLYSIS BY BAKER'S YEAST
Glaenzer, B.I.,Faber, K.,Griengl, H.
, p. 4293 - 4294 (2007/10/02)
Optically active N-acetylamino acid esters were obtained by enantioselective hydrolysis of their racemates using fermenting baker's yeast.