alpha-Actinin interacts specifically with model membranes containing glycerides and fatty acids.

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Abstract
A method was developed to identify specific protein-lipid interactions of complex lipid mixtures and to assess their effect on the arrangement of such complexes in monolayers at an air-water interface. Its application to striated [pig] muscle .alpha.-actinin revealed that just 2 lipids selectively interact with .alpha.-actinin. One molecule of glyceride and 1 molecule of fatty acid were associated in a constant stoichiometry with 1 molecule of the .alpha.-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 .alpha.-actinin liposome mixtures followed by peptide analysis; the peptide patterns of .alpha.-actinin depended on the presence or absence of only these 2 lipids. Possible implications of these findings are discussed in the context of Z-line formation.