Gene/Protein Disease Symptom Drug Enzyme Compound
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A convenient method for passivating and functionalizing stainless steel is described. Several methods of coating stainless steel (SS) samples with silica were investigated and of these methods, a thin (less than 15 nm thick) layer of silica created by atomic layer deposition (ALD) was found to give superior performance in electrochemical testing. These interfaces were then used as a platform for further functionalization with molecules of biological interest. Specifically, the SS samples were functionalized with biologically significant carbohydrates [N-acetyl-D-glucosamine (GlcNAc) and D-galactose (Gal)] that contain trialkoxysilane derivatives as chemical handles for linking to the surface. The presence and biological availability of these moieties on the silica coated SS were confirmed by XPS analysis and an enzyme-linked lectin assay (ELLA) using complementary lectins that specifically recognize the surface-bound carbohydrate. This method has the potential of being adapted to the functionalization of stainless steel biomedical implants with other biologically relevant carbohydrates.
ACS Appl Mater Interfaces 2011 May
PMID:Biocompatible carbohydrate-functionalized stainless steel surfaces: a new method for passivating biomedical implants. 2143 37

The attachment of the sugar N-acetyl-D-glucosamine (GlcNAc) to specific serine and threonine residues on proteins is referred to as protein O-GlcNAcylation. O-GlcNAc transferase (OGT) is the enzyme responsible for carrying out the modification, while O-GlcNAcase (OGA) reverses it. Protein O-GlcNAcylation has been implicated in a wide range of cellular processes including transcription, proteostasis, and stress response. Dysregulation of O-GlcNAc has been linked to diabetes, cancer, and neurodegenerative and cardiovascular disease. OGA has been proposed to be a drug target for the treatment of Alzheimer's and cardiovascular disease given that increased O-GlcNAc levels appear to exert a protective effect. The search for specific, potent, and drug-like OGA inhibitors with bioavailability in the brain is therefore a field of active research, requiring orthogonal high-throughput assay platforms. Here, we describe the synthesis of a novel probe for use in a fluorescence polarization based assay for the discovery of inhibitors of OGA. We show that the probe is suitable for use with both human OGA, as well as the orthologous bacterial counterpart from Clostridium perfringens, CpOGA, and the lysosomal hexosaminidases HexA/B. We structurally characterize CpOGA in complex with a ligand identified from a fragment library screen using this assay. The versatile synthesis procedure could be adapted for making fluorescent probes for the assay of other glycoside hydrolases.
ACS Chem Biol 2018 05 18
PMID:O-GlcNAcase Fragment Discovery with Fluorescence Polarimetry. 2964 Nov 81

Glucosamine, the amino sugar made from glucose, is a safe and natural reagent for post-combustion carbon dioxide capture. Its most plentiful derivative, N-acetylglucosamine (or NAG), was studied in this work with respect to its reaction kinetics in aqueous solutions. A stirred cell reactor with a flat gas-liquid interface was used, and it was found that CO2 reacts with NAG via a pathway similar to that with alkanolamines. In the 20-100 mM range of NAG concentration, the second-order rate constant at T = 308 K was 125 kmol m-3 s-1. For the 303-313 K range, the activation energy was 42 kJ mol-1. In a study on vapor-liquid equilibrium, it was found that the loading capacity of NAG (100 mM) at 303 K was 0.6 mol CO2/mol NAG, while the equilibrium partial pressure of CO2 was 0.8 kPa. Three rate promoters were tested, and piperazine showed better efficacy than monoethanolamine and 2-amino-2-methyl-1-propanol in aqueous NAG solutions. This work is expected to stimulate further interest in this new, green CO2 capturing solvent.
ACS Omega 2020 Oct 27
PMID:Kinetics of Carbon Dioxide Removal Using N-Acetylglucosamine. 3313 64