62377-41-7Relevant articles and documents
Enantioselective, Catalytic Vicinal Difluorination of Alkenes
Scheidt, Felix,Sch?fer, Michael,Sarie, Jér?me C.,Daniliuc, Constantin G.,Molloy, John J.,Gilmour, Ryan
supporting information, p. 16431 - 16435 (2018/11/23)
The enantioselective, catalytic vicinal difluorination of alkenes is reported by II/IIII catalysis using a novel, C2-symmetric resorcinol derivative. Catalyst turnover via in situ generation of an ArIIIIF2 species is enabled by Selectfluor oxidation and addition of an inexpensive HF–amine complex. The HF:amine ratio employed in this process provides a handle for regioselective orthogonality as a function of Br?nsted acidity. Selectivity reversal from the 1,1-difluorination pathway (geminal) to the desired 1,2-difluorination (vicinal) is disclosed (>20:1 in both directions). Validation with electron deficient styrenes facilitates generation of chiral bioisosteres of the venerable CF3 unit that is pervasive in drug discovery (20 examples, up to 94:06 e.r.). An achiral variant of the reaction is also presented using p-TolI (up to >95 % yield).
Arylaminoethyl carbamates as a novel series of potent and selective cathepsin S inhibitors
Tully, David C.,Liu, Hong,Chatterjee, Arnab K.,Alper, Phil B.,Williams, Jennifer A.,Roberts, Michael J.,Mutnick, Daniel,Woodmansee, David H.,Hollenbeck, Thomas,Gordon, Perry,Chang, Jonathan,Tuntland, Tove,Tumanut, Christine,Li, Jun,Harris, Jennifer L.,Karanewsky, Donald S.
, p. 5107 - 5111 (2007/10/03)
We report a novel series of noncovalent inhibitors of cathepsin S. The synthesis of the peptidomimetic scaffold is described and structure-activity relationships of P3, P1, and P1′ subunits are discussed. Lead optimization to a non-peptidic scaffold has r
COMPOUNDS AND COMPOSITIONS AS CATHEPSIN S INHIBITORS
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Page/Page column 22, (2010/02/14)
The invention provides compounds, pharmaceutical compositions comprising such compounds and methods of using such compounds to treat or prevent diseases or disorders associated with the activity of Cathepsin S.
INHIBITORS OF CATHEPSIN S
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Page/Page column 47; 50, (2008/06/13)
The present invention provides compounds, compositions and methods for the selective inhibition of cathepsin S. In a preferred aspect, cathepsin S is selectively inhibited in the presence of at least one other cathepsin isozyme. The present invention also provides methods for treating a disease state in a subject by selectively inhibiting cathepsin S.
INHIBITORS OF CATHEPSIN S
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Page/Page column 39, (2008/06/13)
The present invention provides compounds, compositions and methods for the selective inhibition of cathepsin S. In a preferred aspect, cathepsin S is selectively inhibited in the presence of at least one other cathepsin isozyme. The present invention also
Biocatalytic racemization of aliphatic, arylaliphatic, and aromatic α-hydroxycarboxylic acids
Glueck, Silvia M.,Pirker, Monika,Nestl, Bettina M.,Ueberbacher, Barbara T.,Larissegger-Schnell, Barbara,Csar, Katrin,Hauer, Bernhard,Stuermer, Rainer,Kroutil, Wolfgang,Faber, Kurt
, p. 4028 - 4032 (2007/10/03)
Biocatalytic racemization of a range of aliphatic, (aryl)aliphatic, and aromatic α-hydroxycarboxylic acids was accomplished by using whole resting cells of a range of Lactobacillus spp. The mild (physiological) reaction conditions ensured an essentially "clean" isomerization in the absence of side reactions, such as elimination or decomposition. Whereas straight-chain aliphatic 2-hydroxy-carboxylic acids were racemized with excellent rates (up to 85% relative to lactate), steric hindrance was observed for branched-chain analogues. Good rates were observed for aryl-alkyl derivatives, such as 3-phenyllactic acid (up to 59%) and 4-phenyl-2-hydroxybutanoic acid (up to 47%). In addition, also mandelate and its o-chloro analogue were accepted at a fair rate (45%). This biocatalytic racemization represents an important tool for the deracemization of a number of pharmaceutically important building blocks.
Biocatalytic racemisation of α-hydroxycarboxylic acids at physiological conditions
Glueck, Silvia M.,Larissegger-Schnell, Barbara,Csar, Katrin,Kroutil, Wolfgang,Faber, Kurt
, p. 1904 - 1905 (2007/10/03)
Biocatalytic racemisation of aliphatic, aryl-aliphatic and aromatic α-hydroxycarboxylic acids was accomplished using whole resting cells of Lactobacillus paracasei DSM 20207; the mild (physiological) reaction conditions ensured an essentially 'clean' isomerization in the absence of side reactions, such as elimination or decomposition. The Royal Society of Chemistry 2005.
Inhibitors of protein isoprenyl transferases
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, (2008/06/13)
The present invention relates to novel compounds of Formula I which are useful in inhibiting protein isoprenyl transferases and the farnesylation or geranylgeranylation of the oncogene protein Ras and other related small g-proteins, and compositions containing such compounds and methods of using such compounds.
Inhibitors of protein isoprenyl transferases
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, (2008/06/13)
Compounds having the formula STR1or a pharmaceutically acceptable salt thereof wherein R 1 is (a) hydrogen, (b) loweralkyl, (c) alkenyl, (d) alkoxy, (e) thioalkoxy, (f) halo, (g) haloalkyl, (h) aryl-L 2 --, and (i) heterocyclic-L 2 --; R 2 is selected from STR2(b) --C(O)NH--CH(R 14)--C(O)OR 15, STR3(d) --C(O)NH--CH(R 14)--C(O)NHSO 2 R 16, (e) --C(O)NH--CH(R 14)-tetrazolyl, (f) --C(O)NH-heterocyclic, and (g) --C(O)NH--CH(R 14)--C(O)NR 17 R 18 ; R 3 is heterocyclic, aryl, substituted or unsubstituted cycloalkyl; R 4 is hydrogen, lower alkyl, haloalkyl, halogen, aryl, arylakyl, heterocyclic, or (heterocyclic)alkyl; L 1 is absent or is selected from (a) --L 4 --N(R 5)--L 5 --, (b) --L 4 --O--L 5 --, (c) --L 4 --S(O) n --L 5 -- (d) --L 4 --L 6 --C(W)--N(R 5)--L 5 --, (e) --L 4 --L 6 --S(O)m--N(R 5)--L 5 --, (f) --L 4 --N(R 5)--C(W)--L 7 --L 5 --, (g) --L 4 --N(R 5)--S(O) p --L 7 --L 5 --, (h) optionally substituted alkylene, (i) optionally substituted alkenylene, and (j) optionally substituted alkynylene are inhibitors of protein isoprenyl transferases. Also disclosed are protein isoprenyl transferase inhibiting compositions and a method of inhibiting protein isoprenyl transferases.