The thermodynamic control of protein binding to lipid bilayers for protein chromatography.

A new concept of charge-selective bioseparation with certain advantages over the established ion-exchange technique is reported. The procedure is based on the temperature-controlled creation and dispersion of domain structures in single phospholipid bilayers by means of the phase transition between the gel phase and the fluid phase of the bilayer. The bilayers are presented on a solid support of silica gel. Rather than altering the ionic strength of the buffer, protein elution is accomplished by a change of the chromatography column temperature. The application of temperature gradients improves the protein selectivity of phase transition chromatography.