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The simplest, single-component biological membrane challenges accepted models of macromolecular interactions: lipid lamellar phases swell when immersed in monovalent salt solutions. Moreover, typical of a Hofmeister series, Br salts swell multilayers more than Cl salts, offering an excellent opportunity to investigate long-standing questions of ionic specificity. In accord with earlier measurements of liposome mobilities in electric fields, we find an added electrostatic repulsion of membranes due to anion binding, with a much stronger Br binding compared with Cl. However, contrary to the expectation that electrostatic repulsion should vanish in high salinity, swelling of lipid multilayers is monotonic with increasing salt concentration for both Br and Cl salts. The apparent contradiction is resolved by recognizing that although the electrostatic repulsion is progressively screened by increasing salt concentration, so is the van der Waals (vdW) attraction. Negligible in low salt, weakening of vdW forces becomes significant by the time electrostatic forces vanish. The result is a smooth monotonic swelling curve with no apparent distinction between low and high salt concentration regimes. Furthermore, when compared with theoretical predictions, measured vdW forces decay much too slowly with added salt. However, by accounting for the recently measured salt deficit near lipid bilayers, the expected scaling with Debye screening length is recovered. The combination of ion-specific binding and nonspecific ionic screening of low-frequency fluctuations explains salt effects on lipid membrane interactions and, by extension, explains specific (Hofmeister) effects at macromolecular interfaces between low and high dielectric.

Salt screening and specific ion adsorption determine neutral-lipid membrane interactions