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

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.

Liquid crystal was chosen as an optical probe for the investigation of the interactions of alkyl polyglycosides with proteins at the liquid crystal-aqueous interface. The luminous changes in the LC films were used as a readout.Figure optionsDownload as PowerPoint slide