Controlling the Binding Efficiency of Surface Confined Antibodies through the Design of Mixed Self-Assembled Monolayers

Lucia Sarcina; Pietro Delre; Giovanni Graziano; Angela Stefanachi; Davide Blasi; Rosaria A. Picca; Cinzia Di Franco; Francesco Leonetti; Gaetano Scamarcio; Paolo Bollella; Giuseppe F. Mangiatordi; Eleonora Macchia; Luisa Torsi

doi:10.1002/admi.202300017

Controlling the Binding Efficiency of Surface Confined Antibodies through the Design of Mixed Self-Assembled Monolayers

Lucia Sarcina
, Pietro Delre
, Giovanni Graziano
, Angela Stefanachi
, Davide Blasi
, Rosaria A. Picca
, Cinzia Di Franco
, Francesco Leonetti
, Gaetano Scamarcio
, Paolo Bollella
, Giuseppe F. Mangiatordi^*
, Eleonora Macchia^*
, Luisa Torsi^*

^*Corresponding author for this work

Physics

Research output: Contribution to journal › Article › Scientific › peer-review

13 Citations (Scopus)

39 Downloads (Pure)

Abstract

A plethora of different electronic and optoelectronic devices have been developed lately, for biosensing applications (e.g., label-free, fast, and easier to operate) based on a detecting interface accommodating the biorecognition elements, anchored by thiolate self-assembled monolayers (SAMs) on a gold surface. Here, a surface plasmon resonance (SPR) characterization of anti-p24 anchored on different SAMs is performed to investigate the effect of the SAM structure on the antibodies’ packing efficiency and the sensors’ analytical figures of merit. Notably, the mixed SAM deposited from a solution 10:1 of 3-mercaptopropionic acid and 11-mercaptoundecanoic acid (11MUA) is compared to that resulting from a solution 10:1 of ad hoc synthesized N-(2-hydroxyethyl)-3-mercaptopropanamide (NMPA)/11MUA. Despite the improvement in the anti-p24 surface coverage registered using the 11MUA/NMPA SAM, the latter produces a significant decrease in the antibodies’ binding efficiency against human immunodeficiency virus p24 protein. To provide a molecular rationale behind the SPR data, density functional theory calculations are also undertaken. A comprehensive physical view of the main competing phenomena affecting the biorecognition events at a biofunctionalized gold detecting interface is represented here.

Original language	English
Article number	2300017
Journal	Advanced Materials Interfaces
Volume	10
Issue number	12
DOIs	https://doi.org/10.1002/admi.202300017
Publication status	Published - 24 Apr 2023
MoE publication type	A1 Journal article-refereed

Funding

H2020—Electronic Smart Systems—SiMBiT: Single‐molecule bioelectronic smart system array for clinical testing (Grant agreement ID: 824946), ERCStg 2021 “A binary sensor with single‐molecule digit to discriminate biofluids enclosing zero or at least one biomarker” (NoOne) (Proposal ID 101040383), “PMGB—Sviluppo di piattaforme meccatroniche, genomiche e bioinformatiche per l'oncologia di precisione”—ARS01_01195—PON “RICERCA E INNOVAZIONE” 2014–2020 projects, Åbo Akademi University CoE “Bioelectronic activation of cell functions”, PRIN 17 national project “ACTUAL: At the forefront of Analytical ChemisTry: disrUptive detection technoLogies to improve food safety” (2017RHX2E4), Biosensori analitici usa‐e‐getta a base di transistori organici autoalimentati per la rivelazione di biomarcatori proteomici alla singola molecola per la diagnostica decentrata dell'HIV (6CDD3786), Research for Innovation REFIN—Regione Puglia POR PUGLIA FESR‐FSE 2014/2020, research grant (POR PUGLIA 2/FSE/2020), Center for Colloid and Surface Science, are all acknowledged for partial financial support.

Keywords

density functional theory
HIV1 p24 detection
mixed self-assembled monolayers
surface plasmon resonance

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10.1002/admi.202300017Licence: CC BY

Adv Materials Inter - 2023 - Sarcina - Controlling the Binding Efficiency of Surface Confined Antibodies through the DesignFinal published version, 3.23 MBLicence: CC BY

https://urn.fi/URN:NBN:fi-fe202401314925

Cite this

Sarcina, L., Delre, P., Graziano, G., Stefanachi, A., Blasi, D., Picca, R. A., Di Franco, C., Leonetti, F., Scamarcio, G., Bollella, P., Mangiatordi, G. F., Macchia, E., & Torsi, L. (2023). Controlling the Binding Efficiency of Surface Confined Antibodies through the Design of Mixed Self-Assembled Monolayers. Advanced Materials Interfaces, 10(12), Article 2300017. https://doi.org/10.1002/admi.202300017

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abstract = "A plethora of different electronic and optoelectronic devices have been developed lately, for biosensing applications (e.g., label-free, fast, and easier to operate) based on a detecting interface accommodating the biorecognition elements, anchored by thiolate self-assembled monolayers (SAMs) on a gold surface. Here, a surface plasmon resonance (SPR) characterization of anti-p24 anchored on different SAMs is performed to investigate the effect of the SAM structure on the antibodies{\textquoteright} packing efficiency and the sensors{\textquoteright} analytical figures of merit. Notably, the mixed SAM deposited from a solution 10:1 of 3-mercaptopropionic acid and 11-mercaptoundecanoic acid (11MUA) is compared to that resulting from a solution 10:1 of ad hoc synthesized N-(2-hydroxyethyl)-3-mercaptopropanamide (NMPA)/11MUA. Despite the improvement in the anti-p24 surface coverage registered using the 11MUA/NMPA SAM, the latter produces a significant decrease in the antibodies{\textquoteright} binding efficiency against human immunodeficiency virus p24 protein. To provide a molecular rationale behind the SPR data, density functional theory calculations are also undertaken. A comprehensive physical view of the main competing phenomena affecting the biorecognition events at a biofunctionalized gold detecting interface is represented here.",

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author = "Lucia Sarcina and Pietro Delre and Giovanni Graziano and Angela Stefanachi and Davide Blasi and Picca, \{Rosaria A.\} and \{Di Franco\}, Cinzia and Francesco Leonetti and Gaetano Scamarcio and Paolo Bollella and Mangiatordi, \{Giuseppe F.\} and Eleonora Macchia and Luisa Torsi",

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Sarcina, L, Delre, P, Graziano, G, Stefanachi, A, Blasi, D, Picca, RA, Di Franco, C, Leonetti, F, Scamarcio, G, Bollella, P, Mangiatordi, GF, Macchia, E & Torsi, L 2023, 'Controlling the Binding Efficiency of Surface Confined Antibodies through the Design of Mixed Self-Assembled Monolayers', Advanced Materials Interfaces, vol. 10, no. 12, 2300017. https://doi.org/10.1002/admi.202300017

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AU - Sarcina, Lucia

AU - Delre, Pietro

AU - Graziano, Giovanni

AU - Stefanachi, Angela

AU - Blasi, Davide

AU - Picca, Rosaria A.

AU - Di Franco, Cinzia

AU - Leonetti, Francesco

AU - Scamarcio, Gaetano

AU - Bollella, Paolo

AU - Mangiatordi, Giuseppe F.

AU - Macchia, Eleonora

AU - Torsi, Luisa

PY - 2023/4/24

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AB - A plethora of different electronic and optoelectronic devices have been developed lately, for biosensing applications (e.g., label-free, fast, and easier to operate) based on a detecting interface accommodating the biorecognition elements, anchored by thiolate self-assembled monolayers (SAMs) on a gold surface. Here, a surface plasmon resonance (SPR) characterization of anti-p24 anchored on different SAMs is performed to investigate the effect of the SAM structure on the antibodies’ packing efficiency and the sensors’ analytical figures of merit. Notably, the mixed SAM deposited from a solution 10:1 of 3-mercaptopropionic acid and 11-mercaptoundecanoic acid (11MUA) is compared to that resulting from a solution 10:1 of ad hoc synthesized N-(2-hydroxyethyl)-3-mercaptopropanamide (NMPA)/11MUA. Despite the improvement in the anti-p24 surface coverage registered using the 11MUA/NMPA SAM, the latter produces a significant decrease in the antibodies’ binding efficiency against human immunodeficiency virus p24 protein. To provide a molecular rationale behind the SPR data, density functional theory calculations are also undertaken. A comprehensive physical view of the main competing phenomena affecting the biorecognition events at a biofunctionalized gold detecting interface is represented here.

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KW - HIV1 p24 detection

KW - mixed self-assembled monolayers

KW - surface plasmon resonance

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ER -

Controlling the Binding Efficiency of Surface Confined Antibodies through the Design of Mixed Self-Assembled Monolayers

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