Kastl, Katja and Menke, Manuela and Luethgens, Eike and Faiss, Simon and Gerke, Volker and Janshoff, Andreas and Steinem, Claudia (2006) Partially reversible adsorption of annexin A1 on POPC/POPS bilayers investigated by QCM measurements, SFM, and DMC simulations. CHEMBIOCHEM, 7 (1). pp. 106-115. ISSN 1439-4227, 1439-7633
Full text not available from this repository. (Request a copy)Abstract
The kinetics of annexin A I binding to solid-supported lipid bilayers consisting of 7-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC)/1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine (POPS; 4:7) has been investigated as a function of the calcium ion concentration in the bulk phase. Quartz crystal microbalance measurements in conjunction with scanning force microscopy, fluorescence microscopy, and computer simulations indicate that at a given Ca2+ concentration annexin A1 adsorbs irreversibly on membrane domains enriched in POPS. By contrast, onnexinAl adsorbs reversibly on the POPC-enriched phase, which is composed of single POPS molecules embedded within a POPC matrix. The overall area occupied by the POPS-enriched phase is controlled by the CaCl2 concentration. Monte Carlo simulations suggest that the area of the POPS-enriched phase increases by a factor of 7 when the Ca2+ concentration is changed from 0.01 to I mM.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | CA-2+-DEPENDENT PHOSPHOLIPID-BINDING; SOLID-SUPPORTED MEMBRANES; N-TERMINAL DOMAIN; MEDIATED MEMBRANE; EARLY ENDOSOMES; LIPOCORTIN-I; CALCIUM; AGGREGATION; VISUALIZATION; PHOSPHORYLATION; annexins; calcium; lipid bilayers; membrane proteins; protein binding |
| Subjects: | 500 Science > 540 Chemistry & allied sciences |
| Divisions: | Chemistry and Pharmacy > Institut für Analytische Chemie, Chemo- und Biosensorik |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 01 Mar 2021 10:22 |
| Last Modified: | 01 Mar 2021 10:22 |
| URI: | https://pred.uni-regensburg.de/id/eprint/35099 |
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