Site-directed antibodies immobilization by resorc[4]arene-based immunosensors.

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ID: 102694
2020
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Abstract
One of the main problems in the development of immunosensors is to overcome the complexity of binding antibody to the sensor surface. Most of immobilizing methods lead to a random orientation of antibodies with a lower binding site density and immunoaffinity. In order to control the orientation of antibody immobilization, several resorc[4]arene derivatives were designed and synthesized. After the spectroscopic characterization of resorc[4]arene self-assembled monolayers (SAMs) onto gold films, the surface coverage and the orientation of insulin antibody (Ab-Ins) were assessed by Surface Plasmon Resonance (SPR) technique and compared with a random immobilization method. Experimental results combined with theoretical studies confirmed the dipole-dipole interaction as an important factor in antibody orientation and demonstrated the importance of the upper rim functionalization of resorcarenes. Accordingly, resorcarene 5 showed a major binding force towards Ab-Ins thanks to the H-bond interactions with the amine protein groups. Based on these findings, the resorcarene-based immunosensor is a powerful system with improved sensitivity providing new insight into sensors development.
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quaglio2020sitedirectedchemistry Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Quaglio, Deborah;Mangiardi, Laura;Venditti, Giulia;Del Plato, Cristina;Polli, Francesca;Ghirga, Francesca;Favero, Gabriele;Pierini, Marco;Botta, Bruno;Mazzei, Franco;
Journal Chemistry (Weinheim an der Bergstrasse, Germany)
Year 2020
DOI
10.1002/chem.202000989
URL
Keywords
immunosensor macrocycles surface plasmon resonance resorc[4]arene site directed immobilization

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