Simple and label-free liquid crystal-based sensor for detecting trypsin coupled to the interaction between cationic surfactant and BSA.

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ID: 93799
2018
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Abstract
Trypsin plays a central role in catalyzing the hydrolysis of peptide bonds, so a technique with simple operation is needed to monitor the activity of trypsin. Here a simple and label-free senor based on liquid crystals (LCs) was developed by employing bovine serum albumin (BSA) as the enzyme substrate and dodecyl trimethyl ammonium bromide (DTAB) as the controller for the alignment of LC. It was found that DTAB could form a self-assembled monolayer at the aqueous/LC interface to produce the dark optical images of LCs. And the addition of BSA could disturb the monolayer, so that the optical signal of LCs turned bright from dark. But the hydrolysis of BSA by trypsin resulted in the dark appearance. The sensing platform allows detection as low as 1 U/mL under the polarized light microscope based on at least three measurements. Moreover, this method was successfully applied in the detection of trypsin in human urines, suggesting its potential applications in clinic diagnosis.
Reference Key
wang2018simpletalanta Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Wang, Yi;Zhou, Lele;Kang, Qi;Yu, Li;
Journal Talanta
Year 2018
DOI
S0039-9140(18)30191-7
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