Partitioning of ABA into bilayers of Di-saturated phosphatidylcholines as measured by DSC.

Using differential scanning calorimetry, we have investigated partitioning of the plant hormone abscisic acid into a homologous series of di-saturated phosphatidylcholines increasing in chain length from C(14) to C(19). Partition coefficients calculated from the shift in T(m) range from 1280 for DiC(14)PC to 480 for DiC(19)PC. The free energy of transfer is chain-length independent with a value of DeltaG = -17.4 kJ/mol and an enthalpic contribution of DeltaH = -22.6 kJ/mol. The low net entropic contribution of -TDeltaS = -5.2 J/mol agrees with the concept of the bilayer effect, but differs from that of the entropy-driven classic hydrophobic effect valid for partitioning between bulk solvents. Preferential location of the hormone in the outer region of the membrane is indicated by characteristic changes in the transition profiles and by comparison with partitioning into organic solvents whose dielectric constants model the interior and exterior regions of the bilayer. Differences in partitioning and surface pKa between the biologically active ct-ABA and the inactive tt-isomer are discussed for biological relevance.