73148-70-6Relevant articles and documents
Sulfur(VI) Fluoride Exchange (SuFEx)-Enabled High-Throughput Medicinal Chemistry
Cappiello, John R.,Chen, Emily,Dillon, Nicholas,Hull, Mitchell V.,Kitamura, Seiya,Kitamura, Shinichi,Kotaniguchi, Miyako,Nizet, Victor,Sharpless, K. Barry,Solania, Angelo,Woehl, Jordan L.,Wolan, Dennis W.,Zheng, Qinheng
supporting information, p. 10899 - 10904 (2020/07/13)
Optimization of small-molecule probes or drugs is a synthetically lengthy, challenging, and resource-intensive process. Lack of automation and reliance on skilled medicinal chemists is cumbersome in both academic and industrial settings. Here, we demonstr
N-Sulfonyl dipeptide nitriles as inhibitors of human cathepsin S: In silico design, synthesis and biochemical characterization
Lemke, Carina,Cianni, Lorenzo,Feldmann, Christian,Gilberg, Erik,Yin, Jiafei,dos Reis Rocho, Fernanda,de Vita, Daniela,Bartz, Ulrike,Bajorath, Jürgen,Montanari, Carlos A.,Gütschow, Michael
, (2020/08/07)
A library of cathepsin S inhibitors of the dipeptide nitrile chemotype, bearing a bioisosteric sulfonamide moiety, was synthesized. Kinetic investigations were performed at four human cysteine proteases, i.e. cathepsins S, B, K and L. Compound 12 with a t
Carbohydrates as efficient catalysts for the hydration of α-amino nitriles
Chitale, Sampada,Derasp, Joshua S.,Hussain, Bashir,Tanveer, Kashif,Beauchemin, André M.
supporting information, p. 13147 - 13150 (2016/11/09)
Directed hydration of α-amino nitriles was achieved under mild conditions using simple carbohydrates as catalysts exploiting temporary intramolecularity. A broadly applicable procedure using both formaldehyde and NaOH as catalysts efficiently hydrated a variety of primary and secondary susbtrates, and allowed the hydration of enantiopure substrates to proceed without racemization. This work also provides a rare comparison of the catalytic activity of carbohydrates, and shows that the simple aldehydes at the basis of chemical evolution are efficient organocatalysts mimicking the function of hydratase enzymes. Optimal catalytic efficiency was observed with destabilized aldehydes, and with difficult substrates only simple carbohydrates such as formaldehyde and glycolaldehyde proved reliable.