ArticleBioorganic & medicinal chemistry2026
Incorporation of an alpha-hydroxy substituent modulates activity of triazole bisphosphonate-based geranylgeranyl diphosphate synthase inhibitors.
Article in Bioorganic & medicinal chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Geranylgeranyl diphosphate synthase (GGDPS), the enzyme responsible for producing the isoprenoid substrate used in protein geranylgeranylation reactions, represents a novel therapeutic target in cancer, including malignancies such as multiple myeloma and osteosarcoma. Our work has focused on the development of a series of isoprenoid triazole bisphosphonate-based GGDPS inhibitors. Previous work has revealed that our lead GGDPS inhibitors do achieve substantial systemic distribution, in contrast to clinically used nitrogenous bisphosphonates which accumulate primarily in the bone. We have determined that modifications to these GGDPS inhibitors impact not only potency at the level of the target enzyme, but also activity at cellular and in vivo levels. To explore further this structure-activity relationship, we have prepared a series of novel derivatives that contain an α-hydroxy substituent, but differ based on olefin stereochemistry (E vs Z), length of the isoprenoid side chain (C
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