Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions?

Biological membranes are complex and well-organized multimolecular assembli es composed of a wide variety of protein and lipid molecular species, If su ch a diversity in protein and lipid polar headgroup structures may easily b e related to a large panel of functions, the wide dispersion in acyl chain length and structure which the lipids display is more difficult to understa nd. It is not required for maintaining bilayer assembly and fluidity, Direc t information on the lateral distribution of these various molecular specie s, on their potential specificity for interaction between themselves and,pi th proteins and on the functional implications of these interactions is als o still lacking. Because hydrophobic interactions play a major role in stab ilizing membrane structures, we suggest considering the problem from the po int of view of the matching of the hydrophobic surface of proteins by the a cyl chains of the lipids, After a brief introduction to the hydrophobic mat ching principle, we will present experimental results which demonstrate the predictive power of the current theories and then, we will introduce the n ew and important concept of protein/lipid sorting in membranes, Finally, we will show how the hydrophobic matching condition may play a key role in th e membrane organization and function, (C) 1999 Federation of European Bioch emical Societies.