216235-70-0Relevant academic research and scientific papers
Photoredox-mediated mono- And difluorination of remote unactivated methylene C(sp3)-H bonds of N-alkyl sulfonamides
Deng, Zhiqiang,Zhao, Zhenxiang,He, Gang,Chen, Gong
supporting information, p. 3631 - 3635 (2021/05/31)
A photoredox-mediated δ-C(sp3)-H fluorination of sulfonyl-protected primary alkylamines with Selectfluor is developed. The reaction can proceed in excellent monofluorination selectivity for amine substrates without α substituent. For α-substituted substrates, a slightly modified reaction conditions with two rounds of operation gives the δ,δ-difluorination products in good yield. Mechanistic studies suggest SET oxidation of sulfonamide group directly generates the key sulfonamide N radical intermediate, which triggers a 1,5-HAT process to form the δ alkyl radical.
Inhibitors of protein isoprenyl transferases
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, (2008/06/13)
Compounds having the formula or a pharmaceutically acceptable salt thereof wherein R1is (a) hydrogen, (b) loweralkyl, (c) alkenyl, (d) alkoxy, (e) thioalkoxy, (f) halo, (g) haloalkyl, (h) aryl-L2—, and (i) heterocyclic-L2—; R2is selected from (a) (b) —C(O)NH—CH(R14)—C(O)OR15, (d) —C(O)NH—CH(R14)—C(O)NHSO2R16, (e) —C(O)NH—CH(R14)-tetrazolyl, (f) —C(O)NH-heterocyclic, and (g) —C(O)NH—CH(R14)—C(O)NR17R18; R3is substituted or unsubstituted heterocyclic or aryl, substituted or unsubstituted cycloalkyl or cycloalkenyl, and —P(W)RR3RR3′; R4is hydrogen, lower alkyl, haloalkyl, halogen, aryl, arylakyl, heterocyclic, or (heterocyclic)alkyl; L1is absent or is selected from (a) —L4—N(R5)—L5—, (b) —L4—O—L5—, (c) —L4—S(O)n—L5— (d) —L4—L6—C(W)—N(R5)—L5—, (e) —L4—L6—S(O)m—N(R5)—L5—, (f) —L4—N(R5)—C(W)—L7—L5—, (g) —L4—N(R5)—S(O)p—L7—L5—, (h) optionally substituted alkylene, (i) optionally substituted alkenylene, (j) optionally substituted alkynylene (k) a covalent bond, (l) and (m) are inhibitors of protein isoprenyl transferases. Also disclosed are protein isoprenyl transferase inhibiting compositions and a method of inhibiting protein isoprenyl transferases.
Discovery of CGS 27023A, a non, peptidic, potent, and orally active stromelysin inhibitor that blocks cartilage degradation in rabbits
MacPherson, Lawrence J.,Bayburt, Erol K.,Capparelli, Michael P.,Carroll, Brian J.,Goldstein, Robert,Justice, Michael R.,Zhu, Lijuan,Hu, Shou-Ih,Melton, Richard A.,Fryer, Lynn,Goldberg, Ron L.,Doughty, John R.,Spirito, Salvatore,Blancuzzi, Vincent,Wilson, Doug,O'Byrne, Elizabeth M.,Ganu, Vishwas,Parker, David T.
, p. 2525 - 2532 (2007/10/03)
Structure-activity relationships of a lead hydroxamic acid inhibitor of recombinant human stromelysin were systematically defined by taking advantage of a concise synthesis that allowed diverse functionality to be explored at each position in a template. An ex vivo rat model and an in vivo rabbit model of stromelysin-induced cartilage degradation were used to further optimize these analogs for oral activity and duration of action. The culmination of these modifications resulted in CGS 27023A, a potent, orally active stromelysin inhibitor that blocks the erosion of cartilage matrix.
