A 45 MHz benchtop NMR spectrometer is used to identify the structures and determine the amount of 1-bromoethylbenzene and 1,1-dibromoethylbenzene produced from free-radical bromination of ethylbenzene. The experiment is designed for nonchemistry majors, specifically B.S. Biology students, in a predominantly undergraduate institution with insufficient resources for the initial cost and maintenance of high-field Fourier transform (FT) NMR instrumentation. Students learn the basic concepts of nuclear magnetic resonance, acquire FID (free-induction decay) signals, process the data, interpret, assign peaks, and determine product composition. The experiment demonstrates to students that NMR spectroscopy can be used for molecular structure characterization and for determination of product yields. Hands-on experience with a low-field spectrometer provides undergraduate students with confidence to run an NMR instrument while minimizing fear that can be generated at the sight of high field FT-NMR instrumentation.

Alcohol or ethanol is considered the most widely used recreational drug worldwide, and its production, consumption, and sale are strictly regulated by laws. Alcohol content of alcoholic beverages (wine, beers, and spirits) is about 3–50% v/v. Analytical methods to determine the alcohol content must be reliable, precise, and accurate. In this study, the amount of ethanol in several alcoholic beverages was determined using a 45 MHz low-field benchtop NMR (nuclear magnetic resonance) spectrometer. Internal standard and standard addition analytical methods were utilized to quantify ethanol. For both methods, acetic acid or acetonitrile was used as internal standard to quantify alcohol content by using the peak area corresponding to the methyl peaks of ethanol, acetic acid, or acetonitrile. Results showed that internal standard method gave values of percent alcohol that are in close agreement with the indicated label as confirmed by running the samples in a 400 MHz high-field NMR spectrometer using acetic acid as internal standard. This study demonstrates the utility of a benchtop NMR spectrometer that can provide an alternative technique to analyze percent alcohol in alcoholic products.

The synthesis and characterization of biotinylated chlorin photosensitizer and the corresponding zinc and indium complexes are described for potential applications in photodynamic therapy (PDT) for cancer. Phototoxicity of the biotin-chlorin conjugate and the metallated complexes was determined in colon carcinoma CT26 cell lines known to overexpress biotin (Vit B7) receptors. Cell survival assay indicated that the biotinylated chlorin and indium complex showed increased cell growth inhibition than the zinc complex and the starting chlorin (methyl pheophorbide). Fluorescence microcopy studies revealed the generation of apoptotic cells upon light irradiation of colon cells treated with the indium complex. Targeting biotin receptors in cancer cells can improve specificity of photosensitizers for PDT applications.

is a new communicable disease with a widespread outbreak that affects all populations worldwide triggering a rush of scientific interest in coronavirus research globally. In silico molecular docking experiment was utilized to determine interactions of available compounds with SARS-CoV-2 and angiotensin-converting enzyme 2 (ACE2) complex. Chimera and AutoDock Vina were used for protein-ligand interaction structural analysis. Ligands were chosen based on the known characteristics and indications of the drugs as ACE inhibitors (captopril, enalapril, quinapril, moexipril, benazepril, ramipril, perindopril, zofenopril, fosinopril), as ACE2 blockers (losartan, olmesartan), as blood thinning agent (clopidogrel), as cholesterol-lowering prescriptions (simvastatin, atorvastatin), repurposed medications (dexamethasone, hydroxychloroquine, chloroquine), and as investigational drug (remdesivir). Experimental ACE/ACE2 inhibitors are also included: Sigma ACEI, N-(2-aminoethyl)-1-aziridine-ethanamine (NAAE), nicotianamine (NAM), and MLN-4760 (ACE2 inhibitor). The best docked conformations were all located in the ACE2 protein, 50% docked at the interface with lower scores and only clopidogrel and hydroxychloroquine docked at the spike protein. Captopril, moexipril, benazepril, fosinopril, losartan, remdesivir, Sigma ACEI, NAA, and NAM interacted and docked at the interface of ACE2 and SARS-CoV-2 spike protein complex. This may have significant implication in enhancing our understanding of the mechanism to hinder viral entry into the host organism during infection.