Controlling the Binding Efficiency of Surface Confined Antibodies through the Design of Mixed Self‐Assembled Monolayers. Issue 12 (29th March 2023)

• Record Type: Journal Article
• Authors: Sarcina, Lucia; Delre, Pietro; Graziano, Giovanni; Stefanachi, Angela; Blasi, Davide; Picca, Rosaria A.; Di Franco, Cinzia; Leonetti, Francesco; Scamarcio, Gaetano; Bollella, Paolo; Mangiatordi, Giuseppe F.; Macchia, Eleonora; Torsi, Luisa
• Is Part Of: Advanced materials interfaces. Volume 10:Issue 12(2023)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2023-03-29
• Subjects: density functional theory -- HIV1 p24 detection -- mixed self‐assembled monolayers -- surface plasmon resonance; Materials science -- Periodicals; 620.11
• DOI: 10.1002/admi.202300017
• Languages: English
• ISSNs: 2196-7350

Abstract

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. Abstract : For the first time a clear indication is provided here that less tightly packed surfaces lead to more degrees of freedom in antibodies' biofilm and thus a significant enhancement in the antigen binding efficiency of the assay. Moreover, a physical view of the main competing phenomena affecting the biorecognition events at a biofunctionalized gold detecting interface is provided here.