Effects of Cross-Linked Structure on Temperature-Responsive Hydrophobic Interaction of Poly(N-isopropylacrylamide) Hydrogel-Modified Surfaces with Steroids

Cross-linked poly( N -isopropylacrylamide) (PIPAAm) hydrogel-modified surfaces were prepared to investigate the effects of a three-dimensionally cross-linked structure of PIPAAm layers on both wettability changes and hydrophobic interactions with hydrophobic solutes in response to temperature changes. The temperature-responsive surface was prepared by polymerization of IPAAm in the presence of cross-linker on the substrates on which an azo polymerization initiator was covalently bonded. The PIPAAm hydrogel-modified surface showed temperature-responsive hydrophilic/hydrophobic surface property alterations as demonstrated by a large and discontinuous wettability changes in a range of 27−32 °C, a slightly lower temperature range than the phase transition temperature for soluble PIPAAm in aqueous media. This implies that the dynamic motion in response to temperature for PIPAAm segments in the modified hydrogel is restricted due to the cross-linked structure. The effect of the three-dimensional PIPAAm structure on the separation of hydrophobic steroids was investigated by high-performance liquid chromatography with an aqueous mobile phase. The retention times for steroids with different hydrophobicities were increased as the temperature was raised. Cortisone and prednisolone, those showing close hydrophobicity, were successfully separated at an elevated temperature above 25 °C owing to the amplified hydrophobic interaction of prednisolone compared to that of cortisone with the hydrophobic gel surfaces. The separation of relatively hydrophobic steroids was achieved even at lower temperature. The expanded network of the highly hydrated gel layer allowed the penetration of steroid molecules within the hydrogel layer which resulted in the changes in peak width. The cross-linked structure of PIPAAm hydrogels on substrates strongly influences both surface wettability changes and interaction with hydrophobic steroids in response to temperature due to the restricted dynamic motion of PIPAAm segments in the gel.