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

Zhi-Jian Liao ,  Si-Nan Du ,  Yang Luo ,  Fang Zuo ,  Jian-Bin Luo

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引用本文: Zhi-Jian Liao,  Si-Nan Du,  Yang Luo,  Fang Zuo,  Jian-Bin Luo. Use of liquid crystal to study the interactions of alkyl polyglycosides with gelatin and bovine serum albumin[J]. Chinese Chemical Letters, 2016, 27(6): 852-856. doi: 10.1016/j.cclet.2016.01.025 shu
Citation:  Zhi-Jian Liao,  Si-Nan Du,  Yang Luo,  Fang Zuo,  Jian-Bin Luo. Use of liquid crystal to study the interactions of alkyl polyglycosides with gelatin and bovine serum albumin[J]. Chinese Chemical Letters, 2016, 27(6): 852-856. doi: 10.1016/j.cclet.2016.01.025 shu

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

  • College of Chemistry & Environment Protection Engineering, Southwest University for Nationalities, Chengdu 610041, China

  • 基金项目:

    This work was supported by the National Natural Science Foundation of China (Nos. 51273220, 50903011) and the Project of Postgraduate Degree Construction, Southwest University for Nationalities (No. 2015XWD-S0703).

摘要: 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 LCaqueous 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.

English

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  • 收稿日期:  2015-10-12
  • 修回日期:  2015-12-23
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