161315-45-3Relevant academic research and scientific papers
Novel 1-hydroxypiperazine-2,6-diones as new leads in the inhibition of metalloproteinases
Marques, Sérgio M.,Tuccinardi, Tiziano,Nuti, Elisa,Santamaria, Salvatore,André, Vania,Rossello, Armando,Martinelli, Adriano,Santos, M. Amélia
experimental part, p. 8289 - 8298 (2012/02/05)
New compounds containing a novel zinc-binding group (1-hydroxypiperazine-2, 6-dione, HPD) have been identified as effective inhibitors of matrix metalloproteinases (MMPs), with activities in the nanomolar concentration range. That moiety seemed to bind th
Dual inhibitors of matrix metalloproteinases and carbonic anhydrases: Iminodiacetyl-based hydroxamate-benzenesulfonamide conjugates
Marques, Sérgio M.,Nuti, Elisa,Rossello, Armando,Supuran, Claudiu T.,Tuccinardi, Tiziano,Martinelli, Adriano,Santos, M. Amélia
supporting information; experimental part, p. 7968 - 7979 (2009/12/07)
Matrix metalloproteinases (MMPs) and carbonic anhydrases (CAs) are two classes of zinc enzymes with different roles and catalytic targets, such as the degradation of most of the extracellular matrix (ECM) proteins and the regulation of the CO2/
Asymmetric hydrogenation of N-sulfonylated-α-dehydroamino acids: Toward the synthesis of an anthrax lethal factor inhibitor
Shultz, C. Scott,Dreher, Spencer D.,Ikemoto, Norihiro,Williams, J. Michael,Grabowski, Edward J. J.,Krska, Shane W.,Sun, Yongkui,Dormer, Peter G.,DiMichele, Lisa
, p. 3405 - 3408 (2007/10/03)
(Chemical Equation Presented) A novel and highly enantioselective Ru-catalyzed hydrogenation of N-sulfonylated-α-dehydroamino acids has been discovered and demonstrated in the synthesis of an anthrax lethal factor inhibitor (LFI). Herein, this methodology is used to prepare N-sulfonylated amino acids in up to 98% ee. This unprecedented hydrogenation uses a chiral Ru catalyst rather than Rh as typical for acylated dehydroamino acids and esters, and this work reports the first asymmetric hydrogenation of a tetrasubstituted dehydroamino acid derivative using a Ru catalyst.
PROCESS FOR MAKING N-SULFONATED-AMINO ACID DERIVATIVES
-
Page/Page column 24-25, (2008/06/13)
This invention relates to a process for preparing optically active α -amino acid substrates which are used to make potent lethal factor (LF) inhibitors for the treatment of anthrax. This invention further relates to a process for synthesis of potent LF-inhibitors for the treatment of anthrax. Specifically, the invention concerns a novel, high-yielding and highly enantioselective asymmetric hydrogenation reaction of a tetrasubstituted ene-sulfonamide acid or ester.
Sulfonamide hydroxamates
-
, (2008/06/13)
A compound of the Formula (I): wherein Z, R1, R, and Ar2are as defined in the specification. This invention also relates to sulfonamide compounds of the Formula (I) that are inhibitors of procollagen C-proteinase, pharmaceutical compositions containing them, methods for their use, and methods for preparing the compounds.
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.
