Five-component synthesis of marimastat analogues

Tetrahedron Letters

Volumn 39, Issue 45, 1998, Pages 8333-8334

  Patel, Sanjay ^a   Saroglou, Lydia ^a   Floyd, Chris D ^a   Miller, Andrew ^a   Whittaker, Mark ^a  

^a British Biotech Pharmaceuticals Ltd   (United Kingdom)

Author keywords

Enzyme inhibitors; Hydroxamic acids; Ugi reaction

Indexed keywords

COLLAGENASE; GELATINASE; MARIMASTAT; MARIMASTAT DERIVATIVE; MATRILYSIN; MATRIX METALLOPROTEINASE INHIBITOR; STROMELYSIN; UNCLASSIFIED DRUG; ZINC;

AMINATION; ARTICLE; AUTOMATION; CHEMICAL REACTION KINETICS; DRUG SYNTHESIS; ENZYME INHIBITION; HYDROXYLATION; PROTEIN EXPRESSION; ZINC METABOLISM;

EID: 0032487905     PISSN: 00404039     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0040-4039(98)01828-0     Document Type: Article

References (8)

1. [1] Brown P, Whittaker M. Biotech Médecine, 1998, 9, 11-16.
2. [2] Beckett RP, Whittaker M. Exp. Opin. Ther. Patents, 1998, 8, 259-282.
3. [3] Whittaker M. Curr. Opin. Chemical Biology, 1998, 2, 386-396.
4. [4] Floyd CD, Harnett LA, Miller A, Patel S, Saroglou L, Whittaker M. Synlett, 1998, 637-639.
5. [5] Seebach D, Aebi J, Wasmuth D. Org. Synth. Coll. VII, 153-159.
6. [6] Synthesis of α-hydroxy hydroxamic acids via hydroxylaminolysis of acetonides, Todd R, Courtney S. Unpublished results.
7. [7] Yields are given following purification by automated reverse phase preparative HPLC (except 8a:-precipitated from ether/water) and the compounds which were obtained as 1:1 mixtures of diastereoisomers gave satisfactory analytical and spectral data.
8. 50 values of 10 nM, 60 nM and 3 nM respectively.