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International audience; Quince seed mucilage was used in a combination of sodium alginate to develop sustained-release microspheres of cefixime. Physical characterizations such as FTIR, TGA, DSC, and SEM were performed on the prepared microspheres. The swelling of microspheres was maximum at pH 7.4 and reduced at acidic pH. The average particle size ranged from 679 mu m +/-and nbsp;0.21 to 810 mu m +/-and nbsp;0.31, while the drug encapsulation efficiency range was found as 73.76 +/- 0.24-85.6 3 +/- 0.46. In vitro release profile of QSM-alginate-cefixime microspheres followed Korsmeyer-Peppas model (R-2 = 0.9732-0.9946); and release was non-Fickian as we found value of n > 1. This study reveals the benefits of QSM-alginate microspheres for the sustained release of cefixime without any toxicity and it also improved antibacterial properties. (C)and nbsp;2022 The Authors. Published by Elsevier B.V. on behalf of King Saud University.

In this study, we designed a series of pyrene-based donor-π-donor-π-acceptor compounds (HPTC1-HPTC7) by structural tailoring the reference compound (HPTC) using acceptor units. Nonlinear optical (NLO) properties, frontier molecular orbitals (FMOs), natural bonding orbital (NBO), transition density matric (TDM) analysis, and absorption spectra of reference and proposed derivatives were calculated at M06/6-31G(d,p) functional. All the designed compounds have smaller energy bandgaps than the HPTC compound. Moreover, the designed compounds exhibited larger global softness values than the reference. The absorption maxima of HPTC2, HPTC3, and HPTC7 are blue shifted with respect to HPTC. NBO analysis revealed that prolonged hyper conjugative associations and strong interactions between the donor (π) and acceptor (π*) moieties play a crucial part in their stabilization. The FMO and NBO findings supported the NLO responses of entitled compounds, and consequently, the linear and nonlinear properties of designed derivatives elevate compared to the reference molecule. Promisingly, the NLO response for HPTC7 comprises of highest values of , βtotal and as 1.92 × 10−22 esu, 1.95 × 10−27 esu, and 4.69 × 107 (a.u). This NLO behavior shows push–pull NLO chromophores for HPTC7 predicting its role in pursuing NLO materials for optoelectronic applications.

This study was undertaken to assess the potential of Tribolium castaneum (Red flour beetle) acetylcholinesterase (Tc-AChE) based electrochemical biosensor integrating WO3/g-C3N4 nanocomposite modified Pencil graphite electrode to detect an organophosphate insecticide, Phosmet. The WO3/g-C3N4 nanocomposite provides a non-toxic, biocompatible surface for binding the enzyme on the electrode surface, attributed to its large surface area, high conductivity, and low ohmic resistance. The proposed biosensor shows a very good analytical performance with LOD 3.6 nM for Phosmet and effectively determined Phosmet in wheat with a 99% recovery rate. Furthermore, molecular docking deciphers the binding interactions of Phosmet with Tc-AChE using a modified AutoDock LGA algorithm and an AMBER03 force field in YASARA. The kinetic parameters strongly suggest the high potency of inhibitor with the enzyme. This study presents an adaptable, rapid, and straightforward approach that opens ways towards real progress in developing commercial biosensors for pesticide detection.

Development of biosimilars is costly, where glycan analysis is a significant constraint on time and money. This paper provides an in-depth characterisation of several novel recombinant prokaryotic lectins (RPLs), developed through directed evolution, displaying specific binding activities to α-mannose, β-galactose, fucose and sialic acid residues, tested against major biosimilar targets. The binding characterisation of all lectins was performed employing the principles of bio-layer interferometry (BLI), with help of the streptavidin-coated sensor with the biotinylated lectins. The binding activity of the RPLs and the specificity to a broad range of glycoproteins and glycoconjugates were evaluated and compared to those of equivalent plant-derived lectins. While exhibiting better or similar specificity, RPLs displayed significantly better binding in all cases. The binding mechanisms are explained with particular focus on the role hydrogen bonding plays in the change of specificity for a galactose specific lectin. Furthermore, different sets of RPLs and their plant equivalents were assayed against the different glycoprotein targets to evaluate the analytical parameters of the lectin-glycoprotein interaction. The obtained LoDs reached by the RPLs were lower than those of their plant counterparts apart from one, exhibiting RPL:PL LoD ratios of 0.8, 2.5, 14.2 and 380 for the sets of lectins specific to fucose, α-mannose, β-galactose and sialic acid, respectively. Such enhancement in analytical parameters of RPLs shows their applicability in protein purification and as bioanalytical tools for glycan analysis and biosensor development.