15136-29-5Relevant articles and documents
Sequential One-Pot Synthesis of Dipeptides through the Transient Formation of CDI-N-Protected α-Aminoesters
de Figueiredo, Renata Marcia,Suppo, Jean-Simon,Midrier, Camille,Campagne, Jean-Marc
, p. 1963 - 1968 (2017)
The synthesis of dipeptides through a sequential one-pot procedure from commercially available protected amino acids is described. The transformation relies on the use of in situ generated transiently CDI-protected α-amino esters (CDI, e.g. N,N′-carbonyldiimidazole). In addition of being a highly atom-economical process, the couplings take place under very mild and neutral conditions without adding a base to the reaction medium. This protocol provides a concise and less costly route to dipeptide derivatives (12 examples, up to 87% yield) and is compatible with commonly used N-urethane protecting groups. Moreover, no epimerization was detected even when sensitive Boc-Cys(Bn)?OH was used. (Figure presented.).
Optimization and anti-cancer properties of fluoromethylketones as covalent inhibitors for ubiquitin C-terminal hydrolase L1
Chen, Hao,Das, Chittaranjan,Flaherty, Daniel P.,Galardy, Paul J.,Hewitt, Chad S.,Hussain, Sajjad,Imhoff, Ryan D.,Krabill, Aaron D.,Muli, Christine S.,Wendt, Michael K.
supporting information, (2021/05/31)
The deubiquitinating enzyme (DUB) UCHL1 is implicated in various disease states including neurodegenerative disease and cancer. However, there is a lack of quality probe molecules to gain a better understanding on UCHL1 biology. To this end a study was carried out to fully characterize and optimize the irreversible covalent UCHL1 inhibitor VAEFMK. Structure-activity relationship studies identified modifications to improve activity versus the target and a full cellular characterization was carried out for the first time with this scaffold. The studies produced a new inhibitor, 34, with an IC50 value of 7.7 μM against UCHL1 and no observable activity versus the closest related DUB UCHL3. The molecule was also capable of selectively inhibiting UCHL1 in cells and did not demonstrate any discernible off-target toxicity. Finally, the molecule was used for initial probe studies to assess the role of UCHL1 role in proliferation of myeloma cells and migration behavior in small cell lung cancer cells making 34 a new tool to be used in the biological evaluation of UCHL1.
Cobalt-Catalyzed C(sp2)-H Carbonylation of Amino Acids Using Picolinamide as a Traceless Directing Group
Lukasevics, Lukass,Cizikovs, Aleksandrs,Grigorjeva, Liene
supporting information, p. 2748 - 2753 (2021/04/12)
Herein we report an efficient protocol for the C(sp2)-H carbonylation of amino acid derivatives based on an inexpensive cobalt(II) salt catalyst. Carbonylation was accomplished using picolinamide as a traceless directing group, CO (1 atm) as the carbonyl