Chemoenzymatic synthesis of (1S,2R)-1-amino-2-indanol, a key intermediate of HIV protease inhibitor, indinavir

Date

2000-04-21

Author

Demir, AS
Hamamcı, Haluk
Doganel, F
Ozgul, E

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The synthesis of (1S,2R)-1-amino-2-indanol, a key component of HIV protease inhibitor is accomplished in four steps starting from indanone efficiently and with high levels of diastereo- and enantioselectivity. The starting material is converted into 2-acetoxy-1-indanone involving Manganese (III) acetate oxidation. The 2-acetoxyketone is hydrolyzed to 2-hydroxy-1-indanone enantioselectively using Rhizopus oryzae. Selective reduction of 2-hydroxyoxime derivative, derived from the 2-hydroxyketone, gives the amino alcohol up to 98% diastereo- and enantioselectivity. (C) 2000 Elsevier Science B.V. All lights reserved.

Subject Keywords

Biotransformation, 1-amino-2-indanol, Rhizopus oryzae, enantioselective hydrolysis, Enantioselective reduction

URI

https://hdl.handle.net/11511/29880

Journal

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC

DOI

https://doi.org/10.1016/s1381-1177(99)00092-2

Collections

Graduate School of Natural and Applied Sciences, Article

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An efficient synthesis of (1S, 2R)-1-amino-2-indanol, a key intermediate of HIV protease inhibitor, indinavir Demir, Ayhan Sıtkı; Aksoy-Cam, H; Camkerten, N; Hamamcı, Haluk; Doganel, F (2000-01-01) (1S,2R)-1-amino-2-indanol, a key component of an HIV protease inhibitor is synthesized in four steps starting from indanone. The Mn(OAC)(3) mediated acetoxylation of indanone followed by fungus catalyzed hydrolysis of acetoxyindanone furnished optically pure alpha-hydroxy indanone. Formation and enantioselective reduction of oxime ether of 2-hydroxyindanone afforded (1S, 2R)-1-amino-2-indanol in 97% cis selectivity.
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Citation Formats

A. Demir, H. Hamamcı, F. Doganel, and E. Ozgul, “Chemoenzymatic synthesis of (1S,2R)-1-amino-2-indanol, a key intermediate of HIV protease inhibitor, indinavir,” JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, pp. 157–161, 2000, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/29880.