93200-00-1Relevant articles and documents
Structure-activity analysis of peptidic Chlamydia HtrA inhibitors
Agbowuro, Ayodeji A.,Hwang, Jimin,Peel, Emma,Mazraani, Rami,Springwald, Alexandra,Marsh, James W.,McCaughey, Laura,Gamble, Allan B.,Huston, Wilhelmina M.,Tyndall, Joel D.A.
supporting information, p. 4185 - 4199 (2019/08/07)
Chlamydia trachomatis high temperature requirement A (CtHtrA) is a serine protease that performs proteolytic and chaperone functions in pathogenic Chlamydiae; and is seen as a prospective drug target. This study details the strategies employed in optimizi
Diastereoselective addition of terminal alkynes to chiral nitrones: Asymmetric synthesis of propargylic N-hydroxylamines
Patel, Samir K.,Py, Sandrine,Pandya, Shashi U.,Chavant, Pierre Y.,Vallee, Yannick
, p. 525 - 528 (2007/10/03)
1,3-Asymmetric induction in the Et2Zn-catalyzed addition of terminal alkynes was studied with nitrones bearing a chiral auxiliary on their nitrogen atom. The obtained propargylic N-hydroxylamines were generally isolated in good yields and with satisfactory to excellent diastereoselectivities.
Synthesis of chiral, nonracemic methyleneaziridines derived from β-amino alcohols
Ince, Julie,Ross, Tracey M.,Shipman, Michael,Ennis, David S.
, p. 3397 - 3406 (2007/10/03)
An efficient three step process for the synthesis of chiral, nonracemic methyleneaziridines derived from homochiral β-amino alcohols is described. Methyleneaziridines 4a-e produced using this chemistry have been shown to possess high enantiomeric purities
Probing enzyme stereospecificity. Inhibition of α-chymotrypsin and subtilisin Carlsberg by chiral amine- and aminoalcohol-derivatives
Occhiato, Ernesto,Jones, J. Bryan
, p. 4199 - 4214 (2007/10/03)
Various enantiomeric amine and aminoalcohol amide and α-ketoamide derivatives have been evaluated as competitive inhibitors of the representative serine proteases α-chymotrypsin (CT) and subtilisin Carlsberg (SC). Each compound studied was an effective competitive inhibitor of both enzymes. However, only for the best inhibitor, N-pyruvoyl-1-(1-naphthyl)ethylamine (K1 27 μM for the S-enantiomer with CT), was noteworthy enantiomeric discrimination manifest, with the S-enantiomer being a significantly more powerful inhibitor of CT and SC than its R-counterpart by factors of 12.6- and 73-fold, respectively. The enzyme-inhibitor interactions responsible for this strong binding and enantiomeric discrimination were revealed by molecular modelling analyses.