Open Access System for Information Sharing

Login Library

 

Article
Cited 0 time in webofscience Cited 0 time in scopus
Metadata Downloads

A New Strategy for Reporting Specific Protein Binding Events at Aqueous-Liquid Crystal Interfaces in the Presence of Non-Specific Proteins

Title
A New Strategy for Reporting Specific Protein Binding Events at Aqueous-Liquid Crystal Interfaces in the Presence of Non-Specific Proteins
Authors
Park, C. S.Iwabata, K.Sridhar, U.Tsuei, M.Singh, K.KIM, YOUNGKIThayumanavan, S.Abbott, N. L.
Date Issued
19-Feb-2020
Publisher
AMER CHEMICAL SOC
Abstract
Aqueous-liquid crystal (LC) interfaces offer promise as responsive interfaces at which biomolecular recognition events can be amplified into macroscopic signals. However, the design of LC interfaces that distinguish between specific and non-specific protein interactions remains an unresolved challenge. Herein, we report the synthesis of amphiphilic monomers, dimers, and trimers conjugated to sulfonamide ligands via triazole rings, their assembly at aqueous-LC interfaces, and the orientational response of LCs to the interactions of carbonic anhydrase II (CAII) and serum albumin with the oligomer-decorated LC interfaces. Of six oligomers synthesized, only dimers without amide methylation were found to assemble at aqueous interfaces of nematic 4-cyano-4'-pentylbiphenyl (5CB) to induce perpendicular LC orientations. At dimer-decorated LC interfaces, we found that concentrations of CAII less than 4 mu M did not measurably perturb the LC but prevented non-specific adsorption and penetration of serum albumin into the dimer-decorated interface that otherwise triggered bright, globular LC optical domains. These experiments and others (including competitive adsorption of CAII, BSA, and lysozyme) support our hypothesis that specific binding of CAII to the dimer prevents LC anchoring transitions triggered by non-specific adsorption of serum albumin. We illustrate the utility of the approach by reporting (i) the relative activity of two small-molecule inhibitors (6-ethoxy-2-benzothiazolesulfonamide and benzenesulfonamide) of CAII to sulfonamide and (ii) proteolytic digestion of a protein (CAII) by thermolysin. Overall, the results in this paper provide new insight into the interactions of proteins at aqueous-LC interfaces and fresh ideas for either blocking non-specific interactions of proteins at surfaces or reporting specific binding events at LC interfaces in the presence of non-specific proteins.
Keywords
SELF-ASSEMBLED MONOLAYERS; CARBONIC-ANHYDRASE; SOLID-SURFACES; DESIGN; KINETICS; REORIENTATION; ORGANIZATION; ORIENTATION; ADSORPTION; INHIBITOR
URI
http://oasis.postech.ac.kr/handle/2014.oak/101103
ISSN
1944-8244
Article Type
Article
Citation
ACS APPLIED MATERIALS & INTERFACES, vol. 12, no. 7, page. 7869 - 7878, 2020-02-19
Files in This Item:
There are no files associated with this item.

qr_code

  • mendeley

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Views & Downloads

Browse