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The widespread use of glyphosate and the high dependence of the agricultural industry on this herbicide cause environmental pollution and pose a threat to living organisms. One of the appropriate solutions in sustainable agriculture to deal with pollution caused by glyphosate and its metabolites is creating a symbiotic relationship between plants and mycorrhizal fungi. Glomalin-related soil protein is a key protein for the bioremediation of glyphosate and its metabolite aminomethyl phosphonic acid in soil. This study uses homology modeling, molecular docking, and molecular dynamic simulation approaches to investigate the binding mechanism of glomalin-related soil protein from arbuscular mycorrhiza (GmHsp60) with glyphosate and its metabolite and the role of soil protein in the removal and sequestering of common agricultural soil pollutants. GmHsp60 protein structure was predicted by homology modeling, and the quality of the generated model was assessed. Then, the interaction between glyphosate and aminomethyl phosphonic acid and the modeled GmHsp60 protein was explored by molecular docking. Based on docking results, GmHsp60 has an efficient role in the bioremediation of glyphosate and aminomethyl phosphonic acid (-6.03 and -5.34 kcal/mol). Glyphosate forms three hydrogen bonds with Lys258, Gly262, and Glu58 of GmHsp60, and aminomethyl phosphonic acid forms three hydrogen bonds with Lys258, Gly261, and Gly262 of GmHsp60. In addition, the glyphosate's and its metabolite's stability was confirmed by molecular docking simulations and binding free energy calculations using MM/PBSA analysis. This study provides a molecular-level understanding of GmHsp60 expression and function for glyphosate bioremediation.

Aim: PEGylated anti-Factor D Fab (PEG-aFD) was developed as a potential therapeutic for geographic atrophy, targeting factor D, the rate-limiting enzyme in the alternative complement pathway. An assay was needed to measure total factor D as a pharmacodynamic biomarker in human aqueous humor in the presence of high PEG-aFD concentrations. Results: Commercial kit met sensitivity requirement, but not drug tolerance requirement. In-house ELISA met both drug tolerance and sensitivity requirements. Addition of 100 ng/ml PEG-aFD to the sample diluent enabled accurate measurement of human factor D in the presence of 2.5 mg/ml of PEG-aFD in the in-house ELISA. Conclusion: Accurate measurement of total factor D in human aqueous humor containing high concentrations of PEG-aFD was achieved by adding PEG-aFD to sample diluent.

Background: PEGylation technology is one of long-acting delivery (LAD) platforms used to increase half-life of protein therapeutics. However, PEGylation of anti-Factor D Fab (PEG-aFD) poses challenges for detecting anti-drug antibody (ADA) to both Fab and polyethylene glycol (PEG) portions. Results: Although the bridging ELISA using traditional assay diluent containing Tween 20 is good for detecting ADA to Fab, it failed to detect ADA to PEG. Instead of only reducing Tween 20 in assay diluent, using a proprietary commercial buffer PEG50-1 as assay diluent successfully enabled the detection of ADA to both Fab and PEG with fit-for-purpose sensitivity and drug tolerance. Conclusion: Identification of appropriate assay diluent is critical for detection of ADA to both Fab and PEG in a PEGylated molecule.

Aim: Manual analysis of neck kinematics is usually associated with measurement errors and it requires the use of software capabilities. Considering laboratory usage, software has been developed to solve the associated problems., Materials & Methods: Fluoroscopic images taken from 78 women were used to design and evaluate the performance of the software. The software was implemented using C# language, according to the case-based reasoning technique., Results: The viewpoints of experts suggest accuracy of the software in tracking and calculations, which meets their information requirements., Conclusion: Using the software could help physiotherapists to accomplish their work in decreased time and with improved accuracy., Competing Interests: Financial & competing interests disclosure This work was supported by the Hormozgan University of Medical Sciences (16 July 2016, Grant Number 9405). The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed. No writing assistance was utilized in the production of this manuscript.

Previously, 2-alkylchromans have been introduced as non-azole inhibitors of 14α-demethylase. Accordingly, we incorporated imidazole ring on the 3-position of 2-alkylchromanones to design new inhibitors of 14α-demethylase and potential antifungal agents. Thus, a series of 2-alkyl-3-imidazolylchromanones were synthesized starting from 2-hydroxyphenacyl bromide. The trans-configuration of compounds was confirmed by NMR-spectroscopy. The antifungal activity of title compounds were evaluated against different fungi in comparison with fluconazole and miconazole. trans-2-(1-Pentyl)-3-imidazolylchroman-4-one (4d) showed the most potent activity against yeasts comparable to fluconazole. The experimental data based on (1)H NMR spectroscopy revealed that 2-alkyl side chain and 3-imidazolyl moiety in compound 4d exist predominantly in the di-equatorial conformation. While docking study with 14α-demethylase demonstrated that the di-axial form of compound 4d can be considered as active conformation.