Apolipoprotein B is conformationally flexible but anchored at a triolein/water interface: A possible model for lipoprotein surfaces

Apolipoprotein B (apoB) is one of a unique group of proteins that form and bind to fat droplets, stabilize the emulsified fat, and direct their metabolism. ApoB, secreted on lipoproteins (emulsions), remains bound during lipid metabolism yet exhibits conformational flexibility. It has amphipathic beta-strand (APS)-rich domains and amphipathic alpha-helix (A alpha H)-rich domains. We showed that two consensus APS peptides of apoB bound strongly to hydrophobic interfaces [triolein/water (TO/W) and dodecane/water], were elastic, and were not pushed off the interface when the surface was compressed. In contrast, an AaH peptide modeling helical parts of apoB was forced off the TO/W interface by compression and readsorbed when the interface was expanded. In this report, the surface behavior of apoB-100 was studied at the TO/W interface. Solubilized apoB lowered the interfacial tension of TO/W in a concentration-dependent fashion. At equilibrium tension, if the surface was compressed, part of apoB was pushed off but quickly readsorbed when the surface was expanded. Even when the surface area was compressed by approximate to 55%, part of the apoB molecule remained bound. The maximum surface pressure that apoB could withstand without being partially ejected was 13 mN/m. ApoB showed high elasticity at the TO/W interface. Based on studies of the consensus A beta S and A alpha H peptides, we suggest that A beta Ss anchor apoB and are its nonexchangeable motif, whereas its conformational flexibility arises from both the elastic nature of the APS and the ability of AaH domains of the molecule to desorb and readsorb rapidly in response to surface pressure changes.