Annexin A1 interaction with a zwitterionic phospholipid monolayer: a fluorescence microscopy study.
We present the results of a fluorescence microscopy study of the interaction of annexin A1 with dipalmitoylphosphatidylcholine (DPPC) monolayers as a function of the lipid monolayer phase and the pH of the aqueous subphase. We show that annexin A1-DPPC interaction depends strongly on the domain structure of the DPPC monolayer and only weakly on the subphase pH. Annexin A1 is found to be line active, with preferential adsorption at phase boundaries. Also, annexin A1 is found to form networks in the presence of a domain structure in the monolayer. Our results point toward an important contribution of the unique N-terminal domain to the organization of the protein at the interface.
Freites
J Alfredo
JA
Department of Physics and Astronomy and Institute for Surface and Interface Science, University of California, Irvine, California 92697-4575, USA.
Ali
Shahla
S
Rosengarth
Anja
A
Luecke
Hartmut
H
Dennin
Michael B
MB
D015060:1,2-Dipalmitoylphosphatidylcholine / Q000737:chemistry*; D017305:Annexin A1 / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008856:Microscopy, Fluorescence
D017305:Annexin A1; D015060:1,2-Dipalmitoylphosphatidylcholine