a fluorescent glycolipid-binding peptide probe traces cholesterol dependent microdomain-derived trafficking pathways荧光glycolipid-binding多肽探针痕迹胆固醇依赖microdomain-derived走私通道.pdfVIP

A Fluorescent Glycolipid-Binding Peptide Probe Traces Cholesterol Dependent Microdomain-Derived Trafficking Pathways 1.¤a 1. 1 1 1¤b 1,3 Steffen Steinert , Esther Lee , Guillaume Tresset , Dawei Zhang , Ralf Hortsch , Richard Wetzel , 1 2 2 3 1 Sarita Hebbar , Jeyapriya Raja Sundram , Sashi Kesavapany , Elke Boschke , Rachel Kraut * 1 Institute of Bioengineering and Nanotechnology, A*Star, Singapore, Singapore, 2 Department of Biochemistry, Neurobiology Programme, National University of ¨ Singapore, Singapore, Singapore, 3 Institut fur Lebensmittel- und Bioverfahrenstechnik, Technische Universitaet Dresden, Dresden, Germany Abstract Background: The uptake and intracellular trafficking of sphingolipids, which self-associate into plasma membrane microdomains, is associated with many pathological conditions, including viral and toxin infection, lipid storage disease, and neurodegenerative disease. However, the means available to label the trafficking pathways of sphingolipids in live cells are extremely limited. In order to address this problem, we have developed an exogenous, non-toxic probe consisting of a 25- amino acid sphingolipid binding domain, the SBD, derived from the amyloid peptide Ab, and conjugated by a neutral linker with an organic fluorophore. The current work presents the characterization of the sphingolipid binding and live cell trafficking of this novel probe, the SBD peptide. SBD was the name given to a motif originally recognized by