Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human neutrophil elastase (HNE) is elevated in chronic wounds. Oleic acid albumin formulations that inhibit HNE may be applicable to treatment modalities for chronic wounds. Oleic acid/albumin formulations with mole ratios of 100:1, 50:1, and 25:1 (oleic acid to albumin) were prepared and found to have dose response inhibition properties against HNE. The IC50 values for inhibition of HNE with oleic acid/albumin formulations were 0.029-0.049 microM. Oleic acid/albumin (BSA) formulations were bound to positively and negatively charged cotton wound dressings and assessed for elastase inhibition using a fiber bound formulation in an assay designed to mimic HNE inhibition in the wound. Cotton derivatized with both carboxylate and amine functional groups were combined with oleic acid/albumin formulations at a maximum loading of 0.030 mg oleic acid + 0.14 mg BSA/mg fiber. The IC50 values for inhibition of HNE with oleic acid/albumin formulations bound to derivatized cotton were 0.26-0.42 microM. Release of the oleic acid/albumin formulation from the fiber was measured by measuring oleic acid levels with quantitative GC analysis. Approximately, 35-50% of the fiber bound formulation was released into solution within the first 15 min of incubation. Albumin was found to enhance the rate of elastase hydrolysis of the substrate within a concentration range of 0.3-50 g/L. The acceleration of HNE substrate hydrolysis by albumin required increased concentration of inhibitor in the formulation to obtain complete inhibition of HNE. Oleic acid formulations prepared with albumin enable transport, solubility and promote dose response inhibition of HNE from derivatized cotton fibers under aqueous conditions mimicking the chronic wound.
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PMID:In vitro inhibition of human neutrophil elastase by oleic acid albumin formulations from derivatized cotton wound dressings. 1545 91

The interaction between cis- and trans- RuCl(2)(DMSO)(4) and human serum albumin have been investigated through UV-Vis, circular dichroism, fluorescence spectroscopy and inductively couplet plasma atomic emission spectroscopy (ICP(AES)) method Albumin can specifically bind 1 mole of cis-isomer and 2 moles of the trans-isomer RuCl(2)(DMSO)(4) complex. The interaction of RuCl(2)(DMSO)(4) with HSA causes: a conformational change with the loss of helical stability of protein; the strong quenching of the Trp 214 fluorescence indicating that the conformational change of the hydrophobic binding pocked in subdomain IIA takes place; a local perturbation of the warfarin binding site and induce some conformational changes at neighbour domains, a changing of the binding abilities towards heme.
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PMID:Interaction of Cis- and Trans-RuCl (2)(DMSO)(4) With Human Serum Albumin. 1847 61

Superparamagnetic nanoparticles are of great current interest for biomedical applications in both diagnostics and treatment. Magnetic nanoparticles (MNP) can be manipulated by magnetic fields, so that when functionalized, they can be used for the purification and separation of biomolecules and even whole cells. Here we report combining the separation capabilities of MNPs with the functional (binding) capability of molecularly imprinted polymers. Albumin- creatinine-, lysozyme-, and urea-imprinted polymer nanoparticles were synthesized from poly(ethylene-co-ethylene alcohol) via phase inversion, with both target molecules and hydrophobic magnetic nanoparticles mixed within the polymer solution. Several ethylene:ethylene alcohol mole ratios were studied. The rebinding capacities for those three target molecules varied from 0.76 +/- 0.02 to 5.97 +/- 0.04 mg/g of molecularly imprinted magnetic nanoparticles. Lastly, the composite nanoparticles were used for separation and sensing of template molecules (e.g., human serum albumin) in real samples (urine) and results were compared with a commercial ARCHITECT ci 8200 system.
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PMID:Synthesis of magnetic molecularly imprinted poly(ethylene-co-vinyl alcohol) nanoparticles and their uses in the extraction and sensing of target molecules in urine. 2052 74


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