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1.
Anal Chem ; 95(30): 11254-11262, 2023 08 01.
Article in English | MEDLINE | ID: mdl-37459476

ABSTRACT

Immobilization of proteins onto solid supports has critical industrial, technological, and medical applications, and is a daily task in chemical research. Significant conformational rearrangements often occur due to enzyme-surface interactions, and it is of broad interest to develop methods to probe and better understand these molecular-level changes that contribute to the enzyme's catalytic activity and stability. While circular dichroism is a common method for solution-phase conformational study, the application to surface-supported proteins is not trivial and spatial mapping is not viable. On the other hand, a nonlinear laser spectroscopy technique used to analyze surfaces and interfaces is not often found in most laboratories, therefore requiring an alternative and reliable method. Here, we employed high-dimensional data spectromicroscopy analysis in the infrared region (µ-FTIR) to investigate the enzyme's conformational change when adsorbed onto solid matrices, across a ca. 20 mm2 area. Alcohol dehydrogenase (ADH) enzyme was adopted as a model enzyme to interact with CaF2, Au, and Au-thiol model substrates, strategically chosen for mapping the enzyme dynamics on solid surfaces with different polarity/hydrophobicity properties and extendable to other materials. Two-dimensional chemical maps indicate that the enzyme adsorbs with different patterns in which secondary structures dynamically adjust to optimize interprotein and enzyme-surface interactions. The results suggest an experimental approach to identify and map enzyme conformational dynamics onto different solid surfaces across space and provide insights into immobilized protein structure investigations for areas such as biosensing and bioenergy.


Subject(s)
Proteins , Spectroscopy, Fourier Transform Infrared , Proteins/chemistry , Circular Dichroism , Surface Properties
2.
Anal Bioanal Chem ; 415(18): 3645-3653, 2023 Jul.
Article in English | MEDLINE | ID: mdl-36477496

ABSTRACT

As the global population grows and science and technology development evolve, fulfilling basic human needs has been even more linked to technological solutions. In this review, we present an overview of the biosensor market and discuss the factors that make certain countries more competitive than others in terms of technology and innovation and how this is reflected in the trends in publication and patent filling. Additionally, we expose briefly how the COVID-19 pandemic acts as a catalyst for the integration of research and development, business, and innovation sectors to bring solutions and ideas that have been predicted as tendencies for the future.


Subject(s)
Biosensing Techniques , COVID-19 , Humans , Inventions , Filing , Pandemics
3.
Biosens Bioelectron ; 165: 112428, 2020 Oct 01.
Article in English | MEDLINE | ID: mdl-32729544

ABSTRACT

The manufacture of sensors using large-scale production techniques, such as roll-to-roll (R2R) processing, may fulfill requirements of low-cost disposable devices. Herein, we report the fabrication of fully-printed electrochemical sensors using screen-printed carbon electrodes coated with carbon black inks through slot-die coating within an R2R process. As a proof of concept, sensors were produced to detect the neurotransmitter dopamine with high reproducibility and low limit of detection (0.09 µmol L-1). Furthermore, fully-printed biosensors made with a tyrosinase-containing ink were used to detect catechol in natural water samples. Since slot-die deposition enables printing enzymes without significant activity loss, the biosensors exhibited high stability over a period of several weeks. Even more important, R2R slot-die coating may be extended to any type of sensors and biosensors with the possibility of large-scale manufacturing.


Subject(s)
Biosensing Techniques , Carbon , Electrodes , Ink , Reproducibility of Results
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