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.

Site-directed antibody immobilization by resorc[4]arene-based immunosensors / Quaglio, Deborah; Mangiardi, Laura; Venditti, Giulia; Del Plato, Cristina; Polli, Francesca; Ghirga, Francesca; Favero, Gabriele; Pierini, Marco; Botta, Bruno; Mazzei, Franco. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - (2020). [10.1002/chem.202000989]

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

Quaglio, Deborah;Mangiardi, Laura;Venditti, Giulia;Del Plato, Cristina;Polli, Francesca;Ghirga, Francesca
;
Favero, Gabriele;Pierini, Marco;Botta, Bruno
;
Mazzei, Franco
2020

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.
2020
Resorc[4]arene; site directed immobilization; surface plasmon resonance; immunosensor; macrocycles
01 Pubblicazione su rivista::01a Articolo in rivista
Site-directed antibody immobilization by resorc[4]arene-based immunosensors / Quaglio, Deborah; Mangiardi, Laura; Venditti, Giulia; Del Plato, Cristina; Polli, Francesca; Ghirga, Francesca; Favero, Gabriele; Pierini, Marco; Botta, Bruno; Mazzei, Franco. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - (2020). [10.1002/chem.202000989]
File allegati a questo prodotto
File Dimensione Formato  
Quaglio_Postprint_Site‐directed_2020.pdf

Open Access dal 03/04/2021

Tipologia: Documento in Post-print (versione successiva alla peer review e accettata per la pubblicazione)
Licenza: Tutti i diritti riservati (All rights reserved)
Dimensione 1.47 MB
Formato Adobe PDF
1.47 MB Adobe PDF
Quaglio_Site-directed_2020.pdf

solo gestori archivio

Note: This article also appears in: Hot Topic: Surfaces and Interfaces
Tipologia: Versione editoriale (versione pubblicata con il layout dell'editore)
Licenza: Tutti i diritti riservati (All rights reserved)
Dimensione 5.25 MB
Formato Adobe PDF
5.25 MB Adobe PDF   Contatta l'autore

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1414974
Citazioni
  • ???jsp.display-item.citation.pmc??? 4
  • Scopus 11
  • ???jsp.display-item.citation.isi??? 10
social impact