Interactions of band 3-protein from human erythrocyte membranes with cholesterol and cholesterol analogues

Hoppe Seylers Z Physiol Chem. 1979 Sep;360(9):1225-35. doi: 10.1515/bchm2.1979.360.2.1225.

Abstract

The interaction between cholesterol and band 3-protein from human erythrocyte membranes was studied by incorporating the solubilized protein into monolayers of cholesterol and related sterols at the air-water interface and measuring the changes in surface pressure which accompanied protein incorporation. The following results were obtained: 1) Band 3-protein shows a very strong interaction with cholesterol monolayers. Both apolar and polar bonds contribute to this interaction. 2) Steroids with a structure slightly different from that of cholesterol (especially with respect to the polar group and the side chain) in most cases show a reduced affinity for band 3-protein. Thus, the protein-sterol interaction is highly specific. It is assumed that the protein-cholesterol interaction can be subidivided into two parts: an unspecific one which results from contributions from several sterol molecules, and a specific one which is due to the high affinity binding of the protein and cholesterol. The structural element responsible for the high affinity interaction is assumed to be a sterol-binding niche on the surface of band 3-protein. The sterol is thought to be held in the niche by a hydrogen bond at its polar head and a variety of hydrophobic bonds along its ring system and side chain.

MeSH terms

  • Cholesterol* / analogs & derivatives*
  • Erythrocyte Membrane / analysis*
  • Erythrocytes / analysis*
  • Humans
  • Membrane Proteins* / blood
  • Membranes, Artificial
  • Phosphatidylcholines
  • Pressure
  • Protein Binding
  • Sterols
  • Structure-Activity Relationship
  • Surface Properties

Substances

  • Membrane Proteins
  • Membranes, Artificial
  • Phosphatidylcholines
  • Sterols
  • Cholesterol