Interactions and conformations of alpha-helical human apolipoprotein CI on hydrophilic and on hydrophobic substrates

Article Abstract:

Interactions between amphiphilic alpha-chemical human apolipoprotein CI (APO CI) adsorbed on hydrophilic and on hydrophobic surfaces were studied using an interferometric surface force apparatus in an effort to understand the surface conformation and the binding activity of this protein. Mica was used as the hydrophilic substrate and polymerized octadecyltriethoxysilane (OTE)-covered mica as the hydrophobic substrate.

Methods, Conformational analysis, Hydrophobic effect

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Phase transitions of phospholipid monolayers penetrated by apolipoproteins

Article Abstract:

The ad sorption and monolayer behavior of the exchangeable apolipoproteins, CI and AII, on the phospholipids (DPPC) are studied in a more realistic interface, from a physiological point of view, than the air/highly ionic water interface. A model is developed to understand the phase transitions in the binary systems that have important implications in the understanding of lipoprotein physiology.

Analysis, Phospholipids, Monomolecular films, Chemistry, Physical and theoretical, Physical chemistry

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Phase transitions and conformational changes in monolayers of human apolipoproteins CI and AII

Article Abstract:

Apolipoproteins (APOs) is a special group of proteins that are naturally found on the surface of the blood circulating lipoprotein particles. Proteins with high alpha-helix content, such as APO CI and APO AII, forms Langmuir monolayers at the air/water interface is discussed.

Usage, X-ray diffraction, Atomic force microscopy, Chemical properties

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