| DOI | Resolve DOI: https://doi.org/10.1002/cbic.200400097 |
|---|
| Author | Search for: Murray, Jill; Search for: Cuccia, Louis; Search for: Ianoul, Anatoli1; Search for: Cheetham, James; Search for: Johnston, Linda1 |
|---|
| Affiliation | - National Research Council of Canada. NRC Steacie Institute for Molecular Sciences
|
|---|
| Format | Text, Article |
|---|
| Abstract | 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. |
|---|
| Publication date | 2004 |
|---|
| In | |
|---|
| NPARC number | 12329195 |
|---|
| Export citation | Export as RIS |
|---|
| Report a correction | Report a correction (opens in a new tab) |
|---|
| Record identifier | 337ddbd4-1197-4bce-ac63-a6c9c5507219 |
|---|
| Record created | 2009-09-10 |
|---|
| Record modified | 2020-04-17 |
|---|
