1448459-82-2Relevant academic research and scientific papers
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
, (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.
Asymmetric synthesis of aminopyrimidine and cyclic guanidine amino acids
M?schwitzer, Vicki D.,Kariuki, Benson M.,Redman, James E.
supporting information, p. 4526 - 4528 (2013/08/23)
Syntheses of amino acids with aminopyrimidine and cyclic guanidine side chains are described. The synthetic route employed Heck coupling of methyl 2-acetamidoacrylate to 4-methoxybenzyl protected 2-amino-5-iodopyrimidine, followed by Rh(I)-catalyzed asymm
