6533b82bfe1ef96bd128cd3a

RESEARCH PRODUCT

Formation of irreversibly bound annexin A1 protein domains on POPC/POPS solid supported membranes

Simon FaissAndreas JanshoffKatja KastlClaudia Steinem

subject

Models Moleculargenetic structuresLipid BilayersBiophysicsPhospholipidAnalytical chemistryPhosphatidylserines02 engineering and technologyMicroscopy Atomic ForceBiochemistryBiophysical PhenomenaMembrane Lipids03 medical and health scienceschemistry.chemical_compoundProtein structureSFMMonolayerMicropatterned membranesAnimalsHumansPOPCMonte Carlo simulationAnnexin A1030304 developmental biologyFluorescence microscopy0303 health sciencesEllipsometrytechnology industry and agricultureCell BiologyQuartz crystal microbalanceSurface Plasmon Resonance021001 nanoscience & nanotechnologyBinding constantProtein Structure TertiaryMembraneMicroscopy FluorescencechemistryQCMPhosphatidylcholinesBiophysicsCalciumlipids (amino acids peptides and proteins)Adsorption0210 nano-technologyMonte Carlo MethodProtein BindingAnnexin A1

description

AbstractThe specific interaction of annexin A1 with phospholipid bilayers is scrutinized by means of scanning force and fluorescence microscopy, quartz crystal microbalance, ellipsometry, and modeled by dynamic Monte Carlo simulations. It was found that POPC/POPS bilayers exhibit phase separation in POPC- and POPS-enriched domains as a function of Ca2+ concentration. Annexin A1 interacts with POPC/POPS bilayers by forming irreversibly bound protein domains with monolayer thickness on POPS-enriched nanodomains, while the attachment of proteins to the POPC-enriched regions is fully reversible. A thorough kinetic analysis of the process reveals that both, the binding constant of annexin A1 at the POPC-rich areas as well as the irreversible adsorption rate to the POPS-rich domains increases with calcium ion concentration. Based on the thermodynamic and kinetic data, a possible mechanism of the annexin A1 membrane interaction can be proposed.

yearjournalcountryeditionlanguage
2008-07-01Biochimica et Biophysica Acta (BBA) - Biomembranes
https://doi.org/10.1016/j.bbamem.2008.01.003