Abstract
AbstractThe preparation of enantiopure 2‐(1H‐imidazol‐1‐yl)cycloalkanamines has been studied by independent chemoenzymatic approaches. We first explored a route involving the enzymatic resolution of racemic cycloalkanol analogs for the preparation of the corresponding optically active amines by diverse substitution methodologies including (a) the formation of a mesylated intermediate that could be later substituted by an amine group and (b) the combination of Mitsunobu inversion of the hydroxy group followed by a deprotection step. In order to overcome low isolated yields of the desired optically active amines, racemic‐trans‐2‐(1H‐imidazol‐1‐yl)cycloalkanamines were prepared, and their lipase‐catalyzed enzymatic resolutions were studied. These efforts revealed that lipase from Candida antarctica type B was an efficient biocatalyst. A combination of both chemoenzymatic methodologies has allowed us to obtain the four different enantiopure cis‐ and trans‐(1H‐imidazol‐1‐yl)cycloalkanamine isomers.
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