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Contribution to the Understanding of the Interaction between a Polydopamine Molecular Imprint and a Protein Model: Ionic Strength and pH Effect Investigation

Several studies were devoted to the design of molecularly imprinted polymer (MIP)-based sensors for the detection of a given protein. Here, we bring elements that could contribute to the understanding of the interaction mechanism involved in the recognition of a protein by an imprint. For this purpo...

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Autores principales: Tlili, Amal, Attia, Ghada, Khaoulani, Sohayb, Mazouz, Zouhour, Zerrouki, Chouki, Yaakoubi, Nourdin, Othmane, Ali, Fourati, Najla
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7830185/
https://www.ncbi.nlm.nih.gov/pubmed/33477338
http://dx.doi.org/10.3390/s21020619
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author Tlili, Amal
Attia, Ghada
Khaoulani, Sohayb
Mazouz, Zouhour
Zerrouki, Chouki
Yaakoubi, Nourdin
Othmane, Ali
Fourati, Najla
author_facet Tlili, Amal
Attia, Ghada
Khaoulani, Sohayb
Mazouz, Zouhour
Zerrouki, Chouki
Yaakoubi, Nourdin
Othmane, Ali
Fourati, Najla
author_sort Tlili, Amal
collection PubMed
description Several studies were devoted to the design of molecularly imprinted polymer (MIP)-based sensors for the detection of a given protein. Here, we bring elements that could contribute to the understanding of the interaction mechanism involved in the recognition of a protein by an imprint. For this purpose, a polydopamine (PDA)-MIP was designed for bovine serum albumin (BSA) recognition. Prior to BSA grafting, the gold surfaces were functionalized with mixed self-assembled monolayers of (MUDA)/(MHOH) (1/9, v/v). The MIP was then elaborated by dopamine electropolymerization and further extraction of BSA templates by incubating the electrode in proteinase K solution. Three complementary techniques, electrochemistry, zetametry, and Fourier-transform infrared spectrometry, were used to investigate pH and ionic strength effects on a MIP’s design and the further recognition process of the analytes by the imprints. Several MIPs were thus designed in acidic, neutral, and basic media and at various ionic strength values. Results indicate that the most appropriate conditions, to achieve a successful MIPs, were an ionic strength of 167 mM and a pH of 7.4. Sensitivity and dissociation constant of the designed sensor were of order of (3.36 ± 0.13) µA·cm(−2)·mg(−1)·mL and (8.56 ± 6.09) × 10(−11) mg/mL, respectively.
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spelling pubmed-78301852021-01-26 Contribution to the Understanding of the Interaction between a Polydopamine Molecular Imprint and a Protein Model: Ionic Strength and pH Effect Investigation Tlili, Amal Attia, Ghada Khaoulani, Sohayb Mazouz, Zouhour Zerrouki, Chouki Yaakoubi, Nourdin Othmane, Ali Fourati, Najla Sensors (Basel) Article Several studies were devoted to the design of molecularly imprinted polymer (MIP)-based sensors for the detection of a given protein. Here, we bring elements that could contribute to the understanding of the interaction mechanism involved in the recognition of a protein by an imprint. For this purpose, a polydopamine (PDA)-MIP was designed for bovine serum albumin (BSA) recognition. Prior to BSA grafting, the gold surfaces were functionalized with mixed self-assembled monolayers of (MUDA)/(MHOH) (1/9, v/v). The MIP was then elaborated by dopamine electropolymerization and further extraction of BSA templates by incubating the electrode in proteinase K solution. Three complementary techniques, electrochemistry, zetametry, and Fourier-transform infrared spectrometry, were used to investigate pH and ionic strength effects on a MIP’s design and the further recognition process of the analytes by the imprints. Several MIPs were thus designed in acidic, neutral, and basic media and at various ionic strength values. Results indicate that the most appropriate conditions, to achieve a successful MIPs, were an ionic strength of 167 mM and a pH of 7.4. Sensitivity and dissociation constant of the designed sensor were of order of (3.36 ± 0.13) µA·cm(−2)·mg(−1)·mL and (8.56 ± 6.09) × 10(−11) mg/mL, respectively. MDPI 2021-01-17 /pmc/articles/PMC7830185/ /pubmed/33477338 http://dx.doi.org/10.3390/s21020619 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Tlili, Amal
Attia, Ghada
Khaoulani, Sohayb
Mazouz, Zouhour
Zerrouki, Chouki
Yaakoubi, Nourdin
Othmane, Ali
Fourati, Najla
Contribution to the Understanding of the Interaction between a Polydopamine Molecular Imprint and a Protein Model: Ionic Strength and pH Effect Investigation
title Contribution to the Understanding of the Interaction between a Polydopamine Molecular Imprint and a Protein Model: Ionic Strength and pH Effect Investigation
title_full Contribution to the Understanding of the Interaction between a Polydopamine Molecular Imprint and a Protein Model: Ionic Strength and pH Effect Investigation
title_fullStr Contribution to the Understanding of the Interaction between a Polydopamine Molecular Imprint and a Protein Model: Ionic Strength and pH Effect Investigation
title_full_unstemmed Contribution to the Understanding of the Interaction between a Polydopamine Molecular Imprint and a Protein Model: Ionic Strength and pH Effect Investigation
title_short Contribution to the Understanding of the Interaction between a Polydopamine Molecular Imprint and a Protein Model: Ionic Strength and pH Effect Investigation
title_sort contribution to the understanding of the interaction between a polydopamine molecular imprint and a protein model: ionic strength and ph effect investigation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7830185/
https://www.ncbi.nlm.nih.gov/pubmed/33477338
http://dx.doi.org/10.3390/s21020619
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