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Updated: May 17, 2026
Measuring Membrane Lipid Turnover with the pH-sensitive Fluorescent Lipid Analog ND6
Published on: July 29, 2021
N-methyl-substituted fluorescent DAG-indololactone isomers exhibit dramatic differences in membrane interactions and
Noga Gal1, Sofiya Kolusheva, Noemi Kedei
1Department of Chemistry, Ben Gurion University, Beer Sheva 84105, Israel.
None:
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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