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- W2960409926 abstract "Abstract Understanding lipid-protein interactions in model membranes is a challenging task. Limited information exist to-date regarding the relative influence of hydrophobic and electrostatic forces on the organization of proteins inside model membranes, while these forces determine the structure of lipid-protein complexes. We measured the surface pressure (π) - molecular area (A) isotherm cycles of protein (BSA) – lipid (DMPA) mixed monolayers below and above the isoelectric point of BSA (≈ 4.8). At pH ≈ 4.0, below the isoelectric point, BSA is positively charged, and exposes few hydrophobic groups at its surface, compression-decompression isotherms show a nearly reversible hysteresis. At pH ≈ 7.0, above the isoelectric point, BSA is negatively charged and more hydrophobic. At this pH, compression-decompression isotherms show an irreversible hysteresis. This behaviour indicates that the deformation of BSA molecules under pressure is reversible below the isoelectric point, while it becomes irreversible above it. X-ray reflectivity studies for protein-lipid mixed monolayers show that BSA molecules move from the zone close to water and near the lipid polar heads toward the zone occupied by their hydrocarbon tails s when surface pressure increases. Mostly the surface pressure in combinations with hydrophobic and electrostatic interactions is responsible for such structural modifications." @default.
- W2960409926 created "2019-07-23" @default.
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- W2960409926 date "2019-10-01" @default.
- W2960409926 modified "2023-09-27" @default.
- W2960409926 title "pH-dependent structure, pattern and hysteresis behaviour of lipid (DMPA)-protein (BSA) monolayer complex" @default.
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- W2960409926 doi "https://doi.org/10.1016/j.colsurfa.2019.123663" @default.
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