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New findings reported from University of California describe advances in enzyme research.
According to a study from the United States, "The complex formed from crystallization of human farnesyl pyrophosphate synthase (hFPPS) from a solution of racemic [ 6,7-dihydro-5H-cyclopenta[c]pyridin-7-yl(hydroxy)methylene]bis(phosphonic acid) (NE-10501,8), a chiral analog of the anti-osteoporotic drug risedronate, contained the R enantiomer in the enzyme active site."
"This enantiospecificity was assessed by computer modeling of inhibitor-active site interactions using Autodock 3, which was also evaluated for predictive ability in calculations of the known configurations of risedronate, zoledronate, and minodronate complexed in the active site of hFPPS. In comparison with these structures, the 8 complex exhibited certain differences, including the presence of only one Mg2+, which could contribute to its 100-fold higher IC50," wrote S. Deprele and colleagues, University of California (see also Enzyme Research).
The researchers concluded: "An improved synthesis of 8 is described, which decreases the number of steps from 12 to 8 and increases the overall yield by 17-fold."
Deprele and colleagues published the results of their research in Bioorganic & Medicinal Chemistry Letters (Farnesyl pyrophosphate synthase ...
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Source: HighBeam Research, New findings reported from University of California describe advances...