Abstract
The binding mechanism of a new class of lipid-competitive, ATP non-competitive, p110α isoform-selective PI3K (phosphoinositide 3-kinase) inhibitors has been elucidated. Using the novel technique of isoform reciprocal mutagenesis of non-conserved amino acids in the p110α and p110β isoforms, we have identified three unique binding mechanisms for the p110α-selective inhibitors PIK-75, A-66S and J-32. Each of the inhibitor's p110α-isoform-selective binding was found to be due to interactions with different amino acids within p110. The PIK-75 interaction bound the non-conserved region 2 amino acid p110α Ser(773), A-66S bound the region 1 non-conserved amino acid p110α Gln(859), and J-32 binding had an indirect interaction with Lys(776) and Ile(771). The isoform reciprocal mutagenesis technique is shown to be an important analytical tool for the rational design of isoform-selective inhibitors.
Publication types
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Comparative Study
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acids / genetics
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Amino Acids / metabolism*
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Class I Phosphatidylinositol 3-Kinases
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Class II Phosphatidylinositol 3-Kinases / genetics
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Class II Phosphatidylinositol 3-Kinases / metabolism
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Conserved Sequence / genetics
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Dose-Response Relationship, Drug
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Hydrazones / metabolism
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Hydrazones / pharmacology
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Isoenzymes / antagonists & inhibitors
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Isoenzymes / genetics
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Isoenzymes / metabolism
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Kinetics
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Mutagenesis, Site-Directed*
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Phosphatidylinositol 3-Kinases / genetics
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Phosphatidylinositol 3-Kinases / metabolism*
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Phosphoinositide-3 Kinase Inhibitors*
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Proline / analogs & derivatives*
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Proline / genetics
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Proline / metabolism
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Protein Binding / genetics
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Sulfonamides / metabolism
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Sulfonamides / pharmacology
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Thiazoles / metabolism*
Substances
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Amino Acids
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Hydrazones
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Isoenzymes
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N1-(2-(t-butyl)-4'-methyl-(4,5'-bithiazol)- 2'-yl)pyrrolidine-1,2-dicarboxamide
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PIK 75
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Phosphoinositide-3 Kinase Inhibitors
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Sulfonamides
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Thiazoles
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Proline
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Class I Phosphatidylinositol 3-Kinases
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Class II Phosphatidylinositol 3-Kinases
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p110delta protein, rat