Imaging the Selective Binding of Synapsin to Anionic Membrane Domains

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DOIResolve DOI: http://doi.org/10.1002/cbic.200400097
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TypeArticle
Journal titleChemBioChem
Volume5
Issue11
Pages14891494; # of pages: 6
AbstractSynapsins 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.
Publication date
AffiliationNational Research Council Canada; NRC Steacie Institute for Molecular Sciences
Peer reviewedNo
NPARC number12329195
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Record identifier337ddbd4-1197-4bce-ac63-a6c9c5507219
Record created2009-09-10
Record modified2016-05-09
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