ArticleChembiochem : a European journal of chemical biology2011
N-methyl-substituted fluorescent DAG-indololactone isomers exhibit dramatic differences in membrane interactions and biological activity.
Article in Chembiochem : a European journal of chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Synthesis and Biological Evaluation of Fluorescent Bryostatin Analogues.Chembiochem : a European journal of chemical biology · 2018Article
- Exploring the influence of indololactone structure on selectivity for binding to the C1 domains of PKCα, PKCε, and RasGRP.Bioorganic & medicinal chemistry · 2017Article
- Developmental neurotoxicity of monocrotophos and lead is linked to thyroid disruption.Veterinary world · 2016Article
- Synthesis, biological, and biophysical studies of DAG-indololactones designed as selective activators of RasGRP.Bioorganic & medicinal chemistry · 2014Article
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14 authors.
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Abstract
N-methyl-substituted diacylglycerol-indololactones (DAG-indololactones) are newly synthesized effectors of protein kinase C (PKC) isoforms and exhibit substantial selectivity between RasGRP3 and PKCα. We present a comprehensive analysis of membrane interactions and biological activities of several DAG-indololactones. Translocation and binding activity assays underline significant variations between the PKC translocation characteristics affected by the ligands as compared to their binding activities. In parallel, the fluorescent properties of the ligands were employed for analysis of their membrane association profiles. Specifically, we found that a slight change in the linkage to the indole ring resulted in significant differences in membrane binding and association of the DAG-indololactones with lipid bilayers. Our analysis shows that seemingly small structural modifications of the hydrophobic regions of these biomimetic PKC effectors contribute to pronounced modulation of membrane interactions of the ligands.
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