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Annexin A1 Interaction with a Zwitterionic Phospholipid Monolayer: A Fluorescence Microscopy Study

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J. Alfredo Freites,^† Shahla Ali,^† Anja Rosengarth,^‡ Hartmut Luecke,^‡^§^‖ and Michael B. Dennin*^†

Department of Physics and Astronomy and Institute for Surface and Interface Science, University of California, Irvine, California 92697-4575, and Department of Molecular Biology and Biochemistry, Department of Physiology and Biophysics, and Department of Information and Computer Science, University of California, Irvine, California 92697-3900

Langmuir, 2004, 20 (26), pp 11674–11683

DOI: 10.1021/la049713b

Publication Date (Web): November 19, 2004

Section:

General Biochemistry

Abstract

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.

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