130892-94-3Relevant academic research and scientific papers
Efficient synthesis of new chiral 1,2-benzothiazin-3-one 1,1-dioxide derivatives via lateral lithiation of 3-N-mesitylenesulfonyl-1,3-oxazolidin-2-ones
Ould Aliyenne, Ahmed,Kra?em, Jamil,Kacem, Yakdhane,Ben Hassine, Béchir
, p. 1473 - 1475 (2008/09/18)
Chiral 3-N-mesitylenesulfonyl-1,3-oxazolidin-2-ones 4a-e derived from (l)- and (d)-amino acids 1a-e undergo lateral lithiation with lithium diisopropylamide and TMEDA in anhydrous THF to provide new optically-active 1,2-benzothiazin-3-one 1,1-dioxide deri
Protease inhibitors. Part 7: Inhibition of Clostridium histolyticum collagenase with sulfonylated derivatives of L-valine hydroxamate
Supuran, Claudiu T.,Scozzafava, Andrea
, p. 67 - 76 (2007/10/03)
Sulfonylated L-valine hydroxamate derivatives were obtained by reaction of alkyl/arylsulfonyl halides with the title amino acid, followed by treatment with benzyl chloride, and conversion of the COOH moiety to the CONHOH group. Other derivatives were obtained by reaction of N-benzyl-L- valine with arylisocyanates, arylsulfonylisocyanates or benzoylisothiocyanate, followed by the similar conversion of the COOH into the CONHOH moiety, with hydroxylamine in the presence of carbodiimides. The obtained compounds were assayed as inhibitors of the Clostridium histolyticum collagenase, ChC (EC 3.4.24.3), a zinc enzyme which degrades triple helical collagen. The hydroxamate derivatives were generally 100-500 times more active than the corresponding carboxylates. In the series of synthesized derivatives, substitution patterns leading to best ChC inhibitors were those involving perfluoroalkylsulfonyl- and substituted-arylsulfonyl moieties, such as pentafluorophenylsulfonyl; 3- and 4-protected-aminophenylsulfonyl-; 3- and 4-carboxyphenylsulfonyl-; 3-trifluoromethylphenylsulfonyl; or 1- and 2- naphthyl among others. Similarly to the matrix metalloproteinase hydroxamate inhibitors, ChC inhibitors of the type reported here must incorporate hydrophobic moieties at the P(2') and P(3') subsites, in order to achieve tight binding to the enzyme. Such compounds might lead to drugs useful in the treatment corneal bacterial keratitis. (C) 2000 Elsevier Science B.V.
