Use of liquid crystal to study the interactions of alkyl polyglycosides with gelatin and bovine serum albumin

Abstract In this study, liquid crystal (LC) was used to study the interactions of alkyl polyglycosides (APG) with gelatin and bovine serum albumin (BSA) at the LC-aqueous interface. The LC easily undergo an orientational transition from a homeotropic to a planar state after proteins were in contact to the LC-aqueous interface decorated with APG, thus inducing an optical change from dark to bright. The optical image analysis reveals that the rearrangement rate of APG monolayer is tightly dependent on the concentration and chemical structure of the protein of interest. For example, the rearrangement rate of APG monolayer increases with an increasing gelatin concentration. We also find that the chemical structure of the proteins has a significant impact on the difference in the growth behavior of bright domains in LC.