Kastl, Katja and Ross, Michaela and Gerke, Volker and Steinem, Claudia (2002) Kinetics and thermodynamics of annexin A1 binding to solid-supported membranes: A QCM study. BIOCHEMISTRY, 41 (31). pp. 10087-10094. ISSN 0006-2960
Full text not available from this repository. (Request a copy)Abstract
By means of the quartz crystal microbalance (QCM) technique, the interaction of annexin Al with lipid membranes was quantified using solid-supported bilayers immobilized on gold electrodes deposited on 5 MHz quartz plates. Solid-supported lipid bilayers were composed of a first octanethiol monolayer chemisorbed on gold and a physisorbed phospholipid monolayer obtained from vesicle fusion. This experimental setup enabled us to determine for the first time rate constants and affinity constants of annexin Al binding to phosphatidylserine-containing layers as a function of the calcium ion concentration in solution and the cholesterol content within the outer leaflet of the solid-supported bilayer. The results reveal that a decrease in Ca2+ concentration from 1 mM to 100 muM significantly increases the rate of annexin A] binding to the membrane independent of the cholesterol content. However, the presence of cholesterol in the membrane altered the affinity constants considerably. While the association constant decreases with decreasing Ca2+ concentration in the case of 1-paimitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC)/1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine (POPS) membranes lacking cholesterol, it remains high in the presence of cholesterol.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | VESICLE AGGREGATION; PHOSPHOLIPID-BINDING; LIPID MICRODOMAINS; FOLDING ENERGETICS; TERMINAL DOMAIN; CHOLESTEROL; MUTAGENESIS; MONOLAYERS; MECHANISM; CALCIUM; |
| 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: | 07 Sep 2021 05:27 |
| Last Modified: | 07 Sep 2021 05:27 |
| URI: | https://pred.uni-regensburg.de/id/eprint/39985 |
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