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Lipase-catalysed acylation of prostanoids
1Institute of Chemistry at Tallinn Technical University, Estonia. omar@boc.ic.ee
Bioorganic & Medicinal Chemistry Letters
|July 16, 1999
Summary
Enzymatic acylation regioselectively modified prostaglandins (PG) and cloprostenol at the 11-position. The lipase Novozym 435 demonstrated specific acetylation of these compounds, including enantiospecificity for cloprostenol.
Area of Science:
- Biocatalysis
- Organic Chemistry
- Enzymology
Background:
- Prostaglandins (PG) are crucial lipid compounds with diverse physiological roles.
- Enzymatic modifications offer regioselective and stereoselective synthetic routes.
- Lipases are versatile biocatalysts for acylation reactions.
Purpose of the Study:
- To investigate the regioselective 11-acylation of natural prostaglandins (PGF2alpha, PGE1) and cloprostenol using a lipase catalyst.
- To explore the acylation of the 15-OH group in PGE2 under similar conditions.
- To determine the enantiospecificity of the lipase-catalyzed 11-acetylation of cloprostenol.
Main Methods:
- Regioselective acylation of prostaglandins and cloprostenol using Novozym 435 as a catalyst.
- Vinyl acetate was employed as the acyl donor in the enzymatic reactions.
- Separate treatment of (+)- and (-)-cloprostenol enantiomers to assess enantiospecificity.
Main Results:
- Novozym 435 regioselectively catalyzed the 11-acylation of PGF2alpha, PGE1, and (+)-cloprostenol.
- The 15-OH group of PGE2 was also acylated with significant velocity under the same conditions.
- The lipase exhibited enantiospecificity in the acetylation of cloprostenol enantiomers.
Conclusions:
- Lipase-catalyzed acylation provides an efficient method for regioselective modification of prostaglandins and cloprostenol.
- Novozym 435 shows distinct reactivity towards different hydroxyl groups in prostaglandins.
- The study confirms the utility of enzymatic methods for stereoselective synthesis in prostaglandin chemistry.