Interaction of nominally soluble proteins with phospholipid monolayers at the air-water interface |
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| Authors: | Wayne H Pitcher III Sarah L KellerWray H Huestis |
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| Institution: | a Department of Chemistry, Stanford University, Stanford, CA 94305, USA
b Department of Chemistry, Campus Box 351700, University of Washington, Seattle, WA 98195-1700, USA |
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| Abstract: | The interactions of carbonmonoxyhemoglobin (HbCO), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and polyhistidine with phospholipid monolayers at the air-water interface were studied at physiological pH and ionic strength. HbCO and GAPDH both interact more strongly with monolayers containing negatively charged lipids. The interaction of HbCO and GAPDH with lipid monolayers decreases with increasing pH. Both the HbCO-monolayer and the GAPDH-monolayer interactions can be modeled as diffusion-limited processes, with kinetic data fit to a stretched exponential equation. The significance of these kinetics are discussed. Polyhistidine interacts only with monolayers containing lipids with negatively charged headgroups. In total, the results presented are consistent with an HbCO-lipid interaction with a large electrostatic component, a GAPDH-lipid interaction with comparable electrostatic and hydrophobic components, and a polyhistidine-lipid interaction that is solely electrostatic. |
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| Keywords: | Protein-lipid interaction Air-water interface Hemoglobin Glyceraldehyde-3-phosphate dehydrogenase Phospholipid Monolayer |
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