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Imaging the Selective Binding of Synapsin to Anionic Membrane Domains
Author(s) -
Murray Jill,
Cuccia Louis,
Ianoul Anatoli,
Cheetham James J.,
Johnston Linda J.
Publication year - 2004
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200400097
Subject(s) - synapsin , synaptic vesicle , vesicle , biophysics , chemistry , synapsin i , lipid bilayer , static electricity , membrane , atomic force microscopy , electrostatics , membrane protein , nanotechnology , biochemistry , materials science , biology , electrical engineering , engineering
Synapsins are membrane‐associated proteins that cover the surface of synaptic vesicles and are responsible for maintaining a pool of neurotransmitter‐loaded vesicles for use during neuronal activity. We have used atomic force microscopy (AFM) to study the interaction of synapsin I with negatively charged lipid domains in phase‐separated supported lipid bilayers prepared from mixtures of phosphatidylcholines (PCs) and phosphatidylserines (PSs). The results indicate a mixture of electrostatic binding to anionic PS‐rich domains as well as some nonspecific binding to the PC phase. Interestingly, both protein binding and scanning with synapsin‐coated AFM tips can be used to visualize charged lipid domains that cannot be detected by topography alone.