97614-41-0Relevant articles and documents
SITE-SPECIFIC ANTIBODY-DRUG CONJUGATES BY ADP-RIBOSYL CYCLASES
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Page/Page column 37; 39, (2021/11/13)
Antibody-drug conjugates, compositions thereof, and methods use. The antibody-drug conjugates include a fusion protein comprising an antibody covalently linked to an ADP-ribosyl cyclase protein via a peptide linker moiety at one or more of a C-terminus or N-terminus of a heavy or light chain of the antibody, a NAD or NMN analogue, and a payload such that the NAD or NMN analogue is conjugated to both the payload and the ADP-ribosyl cyclase protein.
Isolation, synthesis, and characterization of impurities and degradants from the clofarabine process
Anderson, Bruce G.,Bauta, William E.,Cantrell Jr., William R.,Engles, Tracy,Lovett, Dennis P.
, p. 1229 - 1237 (2013/01/03)
The identification of clofarabine process impurities and their subsequent isolation, synthesis, and characterization is described. Two isomeric process impurities resulting from N6-attachment of a fluoroarabinose to clofarabine were found. Clofarabine's base degradation products, which were different from the process impurities, were also synthesized and characterized. These compounds resulted from modifications to the sugar moiety, the purine ring, or both. A mechanistic rationale for the formation of the various process impurities and degradation products is provided.
Synthesis and NMR conformational studies of stable analogues of 2-deoxy-α-D-ribose-1-phosphate
Rubira, Maria-Jose,Jimeno, Maria-Luisa,Balzarini, Jan,Camarasa, Maria-Jose,Perez-Perez, Maria-Jesus
, p. 8223 - 8240 (2007/10/03)
Malonate ethers and phosphonate derivatives of 2-deoxyribose and 2-deoxy-2-fluoroarabinose have been synthesized, for the first time, as stable analogues of 2-deoxy-α-D-ribose-1-phosphate (1). In almost all the cases, the α-anomers have been obtained as the major isomers. The NMR conformational analysis performed indicate a similar conformational equilibria for the natural phosphate 1 and the here described analogues, with the exception of the glycosyl phosphonate 3α. None of the compounds were inhibitory to purified E. coli thymidine phosphorylase at 250 μM. Also, when administered to intact CEM cells, no inhibitory effect was observed in hypoxanthine and inosine metabolising enzymes, including purine nucleoside phosphorylase.