α -actinin Interacts Specifically with Model Membranes Containing Glycerides and Fatty Acids

A method was developed to identify specific protein--lipid interactions of complex lipid mixtures and to assess their effect upon the arrangement of such complexes in monolayers at an air--water interface. Its application to striated muscle α -actinin revealed that just two lipids selectively interact with α -actinin. One molecule of glyceride and one molecule of fatty acid were found to be associated in a constant stoichiometry with one molecule of the α -actinin dimer. In the presence of both glycerides and fatty acids unexpectedly rigid monolayer areas formed. This lipid specificity could be confirmed by brief protease digestion of α actinin liposome mixtures followed by peptide analysis; the peptide patterns of α -actinin depended on the presence or absence of only these two lipids. Possible implications of these findings are discussed in the context of Z-line formation.