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In recent years, research into the field of materials for flexible sensors and fabrication techniques directed towards wearable devices has helped to raise awareness of the need for new sensors with healthcare applicability. Our goal was to create a wearable flexible pressure sensor that could be integrated into a clinically approved blood pressure monitoring device. The sensor is built from a microfluidic channel encapsulated between two polymer layers, one layer being covered by metal transducers and the other being a flexible membrane containing the microfluidic channel, which also acts as a sealant for the structure. The applied external pressure deforms the channel, causing changes in resistance to the microfluidic layer. Electrical characterization has been performed in 5 different configurations, using alternating current (AC) and (DC) direct current measurements. The AC measurements for the fabricated pressure sensor resulted in impedance values at tens of hundreds of kOhm. Our sensor proved to have a high sensitivity for pressure values between 0 and 150 mm Hg, being subjected to repeatable external forces. The novelty presented in our work consists in the unique technological flow for the fabrication of the flexible wearable pressure sensor. The proposed miniaturized pressure sensor will ensure flexibility, low production cost and ease of use. It is made of very sensitive microfluidic elements and biocompatible materials and can be integrated into a wearable cuffless device for continuous blood pressure monitoring.

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Binding of a newly synthesized indanedione derivative, 2-(2-hydroxy-3-ethoxybenzylidene)-1,3-indanedione (HEBID), to human and bovine serum albumins (HSA and BSA), under simulated physiological conditions was monitored by fluorescence spectroscopy. The binding parameters (binding constants and number of binding sites) and quenching constants were determined according to literature models. The quenching mechanism was assigned to a Förster non-radiative energy transfer due to the HEBID-SA complex formation. A slightly increased affinity of HEBID for HSA was found, while the number of binding sites is approximately one for both albumins. The molecular distance between donor (albumin) and acceptor (HEBID) and the energy transfer efficiency were estimated, in the view of Förster’s theory. The effect of HEBID on the protein conformation was investigated using circular dichroism and synchronous fluorescence spectroscopies. The results revealed partial unfolding in the albumins upon interaction, as well as changes in the local polarity around the tryptophan residues.