Lipid-membrane affinity of chimeric metal-binding green fluorescent protein

The Journal of Membrane Biology
Virapong PrachayasittikulH J Galla

Abstract

The Green Fluorescent Protein (GFP) is a useful marker to trace the expression of cellular proteins. However, little is known about changes in protein interaction properties after fusion to GFP. In this study, we present evidence for a binding affinity of chimeric cadmium-binding green fluorescent proteins to lipid membrane. This affinity has been observed in both cellular membranes and artificial lipid monolayers and bilayers. At the cellular level, the presence of Cd-binding peptide promoted the association of the chimeric GFP onto the lipid membrane, which declined the fluorescence emission of the engineered cells. Binding affinity to lipid membranes was further investigated using artificial lipid bilayers and monolayers. Small amounts of the chimeric GFP were found to incorporate into the lipid vesicles due to the high surface pressure of bilayer lipids. At low interfacial pressure of the lipid monolayer, incorporation of the chimeric Cd-binding GFP onto the lipid monolayer was revealed. From the measured lipid isotherms, we conclude that Cd-binding GFP mediates an increase in membrane fluidity and an expansion of the surface area of the lipid film. This evidence was strongly supported by epifluorescence microscopy, showing...Continue Reading

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Citations

Aug 4, 2009·Biological Trace Element Research·Chartchalerm Isarankura-Na-AyudhyaVirapong Prachayasittikul
Jan 17, 2017·Langmuir : the ACS Journal of Surfaces and Colloids·G BhattacharyaS K Ghosh
Feb 15, 2007·Journal of Computational Chemistry·Chanin NantasenamatVirapong Prachayasittikul

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