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Telomerase is a cellular endogenous reverse transcriptase that uses its internal RNA as a template for extension of the telomere repeat, thus maintaining telomere length. In order to clarify the susceptibility of telomerase to triphosphate derivatives of carbocyclic oxetanocins, inhibition by 9-[trans-trans-2,3-bis(hydroxymethyl)cyclobutyl]guanine triphosphate (C.OXT-GTP) and its methylene analog, 9-(cis-3-hydroxymethyl-2-methylenecyclobutyl)guanine triphosphate (m-C.OXT-GTP) was investigated. Both compounds showed potent inhibitory activity. Lineweaver-Burk plot analyses showed that the inhibition mode of these compounds was competitive with dGTP, the Ki values for C.OXT-GTP and m-C.OXT-GTP being 2.0 microM and 4.9 microM, respectively, and thus smaller than the Km of dGTP (11 microM).

Inhibition of vertebrate telomerases by the triphosphate derivatives of carbocyclic oxetanocin analogs