7682-14-6Relevant 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.
Application of aminoacylase I to the enantioselective resolution of α-amino acid esters and amides
Youshko, Maxim I.,Van Langen, Luuk M.,Sheldon, Roger A.,Svedas, Vytas K.
, p. 1933 - 1936 (2007/10/03)
Aminoacylase I from Aspergillus melleus, a readily available and inexpensive enzyme mainly used in the industrial production of enantiopure L-amino acids from their N-acetyl derivatives, is shown to hydrolyze the esters and amides of natural and non-natural amino acids with high enantioselectivity (for the ester hydrolysis, E is up to 76, in case of amides E >300). The reaction rates of amide and ester hydrolysis are comparable, and in some cases these conversions proceeded even faster than 'traditional' aminoacylase- catalyzed hydrolysis of N-acetyl derivatives thus providing new possibilities for the resolution of the corresponding racemates. This novel approach provides an alternative route for the biocatalytic production of optically active amino acids and their derivatives.
Synthesis of N-Acetyl-α-aminobutyric Acid via Amidocarbonylation: A Case Study
Goerdes, Dirk,Neumann, Helfried,Von Wangelin, Axel Jacobi,Fischer, Christine,Drauz, Karlheinz,Krimmer, Hans-Peter,Beller, Matthias
, p. 510 - 516 (2007/10/03)
The synthesis of N-acetyl-α-aminobutyric acid by amidocarbonylation of propionaldehyde with acetamide in the presence of palladium catalysts is studied in detail. The influence of various reaction conditions and compositions (e.g., the co-catalysts acid and bromide) on the yield of N-acetyl-α-aminobutyric acid is shown. For the first time it is demonstrated that the palladium-catalyzed amidocarbonylations of aldehydes can be run with significantly lower halide concentrations (a major yield decrease. While phosphine-free catalyst systems give best yields at low CO pressure, phosphine-ligated palladium catalysts lead to better yields at higher CO pressure. At low palladium loadings (0.1 mol %), unwanted condensation reactions of propionaldehyde become increasingly competitive.