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Cortisol is a clinically validated stress biomarker that takes part in many physiological and psychological functions related to the body's response to stress factors. In particular, it has emerged as a pivotal tool for understanding stress levels and overall well-being. Usually, in clinics, cortisol levels are monitored in blood or urine, but significant changes are also registered in sweat and saliva. In this work, a surface plasmon resonance probe based on a D-shaped plastic optical fiber was functionalized with a glucocorticoid receptor exploited as a highly efficient bioreceptor specific to cortisol. The developed plastic optical fiber biosensor was tested for cortisol detection in buffer and artificial saliva. The biosensor response showed very good selectivity towards other hormones and a detection limit of about 59 fM and 96 fM in phosphate saline buffer and artificial saliva, respectively. The obtained detection limit, with a rapid detection time (about 5 min) and a low-cost sensor system, paved the way for determining the cortisol concentration in saliva samples without any extraction process or sample pretreatment via a point-of-care test. [ABSTRACT FROM AUTHOR]

Molecularly imprinted polymers (MIPs) are high affinity robust synthetic receptors, which can be optimally synthesized and manufactured more economically than their biological equivalents (i.e. antibody). In MIPs production, rational design based on molecular modeling is a commonly employed technique. This mostly aids in (i) virtual screening of functional monomers (FMs), (ii) optimization of monomer-template ratio, and (iii) selectivity analysis. We present MIRATE, an integrated science gateway for the intelligent design of MIPs. By combining and adapting multiple state-of-the-art bioinformatics tools into automated and innovative pipelines, MIRATE guides the user through the entire process of MIPs’ design. The platform allows the user to fully customize each stage involved in the MIPs’ design, with the main goal to support the synthesis in the wet-laboratory. Availability: MIRATE is freely accessible with no login requirement at http://mirate.di.univr.it/. All major browsers are supported.

One of the difficulties with using molecularly imprinted polymers (MIPs) and other electrically insulating materials as the recognition element in electrochemical sensors is the lack of a direct path for the conduction of electrons from the active sites to the electrode. We have sought to address this problem through the preparation and characterization of novel hybrid materials combining a catalytic MIP, capable of oxidizing the template, catechol, with an electrically conducting polymer. In this way a network of 'molecular wires' assists in the conduction of electrons from the active sites within the MIP to the electrode surface. This was made possible by the design of a new monomer that combines orthogonal polymerizable functionality;, comprising an aniline group and a methacrylamide. Conducting films were prepared on the surface of electrodes (Au on glass) by electropolymerization of the aniline moiety. A layer of MIP was photochemically grafted over the polyaniline, via N,N'-diethyldithiocarbamic acid benzyi ester (iniferter) activation of the methacrylamide groups. Detection of catechol by the hybrid-MIP sensor was found to be specific, and catechol oxidation was detected by cyclic voltammetry at the optimized operating conditions: potential range -0.6 V to +0.8 V (vs Ag/AgC1), scan rate 50 mV/s, PBS pH 7.4. The calibration curve for catechol was found to be linear to 144 pM, with a limit of detection of 228 nM. Catechol and dopamine were detected by the sensor, whereas analogues and potentially interfering compounds, including phenol, resorcinol, hydroquinone, serotonin, and ascorbic acid, had minimal effect ([less than or equal to] 3%) on the detection of either analyte. Non-imprinted hybrid electrodes and bare gold electrodes failed to give any response to catechol at concentrations below 0.5 mM. Finally, the catalytic properties of the sensor were characterized by chronoamperometry and were found to be consistent with Michaelis--Menten kinetics.

Results demonstrate that the chicken liver basic fatty acid-binding protein is significantly different from the mammalian liver fatty acid-binding protein in terms of its relative affinity for different fatty acids and the number of bound ligands. Furthermore, chicken protein shows some similarity to catfish liver fatty acid-binding protein.