Assessment of Gold Bio-Functionalization for Wide-Interface Biosensing Platforms

Publication year: 2020
Authors: Sarcina L. 1,Torsi L. 123, Picca R.A. 12, Manoli K. 12*, Macchia E. 3
Affiliations:
1 - Dipartimento di Chimica, Università degli Studi di Bari Aldo Moro, 70125 Bari, Italy
2 - CSGI (Centre for Colloid and Surface Science), Department of Chemistry, 70125 Bari, Italy
3 - The Faculty of Science and Engineering, Åbo Akademi University, FI-20500 Turku, Finland

 

Published in: Sensors, 2020, Vol. 20, p. 3678
doi: 10.3390/s20133678

The continuous improvement of the technical potential of bioelectronic devices for biosensing applications will provide clinicians with a reliable tool for biomarker quantification down to the single molecule. Eventually, physicians will be able to identify the very moment at which the illness state begins, with a terrific impact on the quality of life along with a reduction of health care expenses. However, in clinical practice, to gather enough information to formulate a diagnosis, multiple biomarkers are normally quantified from the same biological sample simultaneously. Therefore, it is critically important to translate lab-based bioelectronic devices based on electrolyte gated thin-film transistor technology into a cost-effective portable multiplexing array prototype. In this perspective, the assessment of cost-effective manufacturability represents a crucial step, with specific regard to the optimization of the bio-functionalization protocol of the transistor gate module. Hence, we have assessed, using surface plasmon resonance technique, a sustainable and reliable cost-effective process to successfully bio-functionalize a gold surface, suitable as gate electrode for wide-field bioelectronic sensors. The bio-functionalization process herein investigated allows to reduce the biorecognition element concentration to one-tenth, drastically impacting the manufacturing costs while retaining high analytical performance.


MP-SPR keywords: amino coupling, biosensor development, bound mass, protein immobilization