Model of peripheral protein adsorption to the water/lipid interface

J Phys Chem B. 2007 Apr 26;111(16):4073-81. doi: 10.1021/jp065342r. Epub 2007 Mar 30.

Abstract

Two models have been developed to describe the adsorption of a model peripheral protein, colipase, to phospholipid/diacylglycerol (PL/DG) monolayers. One model is applicable at monolayer collapse pressure and at any composition that exceeds the DG mole fraction of PL/DG lateral complexes (Sugár, I. P.; Mizuno, N. K.; Momsen, M. M.; Brockman, H. L. Biophys. J. 2001, 81, 3387-3397). The other model is applicable at any lateral pressure but only below the mole fraction of DG in the complex (Sugár, I. P.; Mizuno, N. K.; Brockman, H. L. Biophys. J. 2005, 89, 3997-4005). Both models assume that initiation of colipase adsorption to the water/lipid interface requires an area of water-exposed hydrophobic surface that exceeds a critical value. In the first model, accessible surface is provided by the head groups of the uncomplexed DG molecules. This surface area follows a binomial distribution. In the second model, accessible area is created by hydrocarbon chains becoming exposed at the water/lipid interface as total lipid packing density of monolayers of PL and/or PL/DG complexes is decreased. This surface area follows a Poisson distribution. The model described in this paper is a unification, extension, and improvement of these models that is applicable at any lateral pressure and any PL/DG mole fraction. Calculated normalized initial colipase adsorption rates are compared with the available experimental values, and predictions of the adsorption rates are made for currently unmeasured compositions and lateral pressure regimes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Lipids / chemistry*
  • Proteins / chemistry*
  • Water / chemistry*

Substances

  • Lipids
  • Proteins
  • Water