English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

In this study, we investigated the use of liquid crystals to selectively detect the activity of enzymes at interfaces decorated with oligopeptide-based membranes. We prepared a mixed monolayer of tetra(ethylene glycol)-terminated lipids and carboxylic acid-terminated lipids at the aqueous-liquid crystal (LC) interface. The 17 amino-acid oligopeptide SNFKTIYDEANQFATYK was then immobilized onto this mixed monolayer through N-hydroxysuccinimide-activation of the carboxylic acid groups. We examined the orientational behavior of nematic 4-cyano-4’-pentylbiphenyl (5CB) after conjugation of the 17 amino-acid oligopeptide with the mixed monolayer assembled at the interface. Immobilization of the oligopeptide caused orientational transitions in 5CB, with a change from homeotropic (perpendicular) to tilted alignment, which was primarily due to the reorganization of the monolayer. The orientation of the 5CB molecules returned to its homeotropic state after contacting the interface containing α-chymotrypsin, which can cleave the immobilized oligopeptide. Control experiments confirmed that the enzymatic activity of α-chymotrypsin triggered the ordering transitions in the LC. These results suggest that the LC can provide a facile method for selective detection of enzymatic activity.

Liquid Crystal-based Imaging of Enzymatic Reactions at Aqueous-liquid Crystal Interfaces Decorated with Oligopeptide Amphiphiles