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1.
J Am Chem Soc ; 143(46): 19542-19550, 2021 11 24.
Artículo en Inglés | MEDLINE | ID: mdl-34752701

RESUMEN

Hydrogen selenide (H2Se) is a central metabolite in the biological processing of selenium for incorporation into selenoproteins, which play crucial antioxidant roles in biological systems. Despite being integral to proper physiological function, this reactive selenium species (RSeS) has received limited attention. We recently reported an early example of a H2Se donor (TDN1042) that exhibited slow, sustained release through hydrolysis. Here we expand that technology based on the P═Se motif to develop cyclic-PSe compounds with increased rates of hydrolysis and function through well-defined mechanisms as monitored by 31P and 77Se NMR spectroscopy. In addition, we report a colorimetric method based on the reaction of H2Se with NBD-Cl to generate NBD-SeH (λmax = 551 nm), which can be used to detect free H2Se. Furthermore, we use TOF-SIMS (time of flight secondary ion mass spectroscopy) to demonstrate that these H2Se donors are cell permeable and use this technique for spatial mapping of the intracellular Se content after H2Se delivery. Moreover, these H2Se donors reduce endogenous intracellular reactive oxygen species (ROS) levels. Taken together, this work expands the toolbox of H2Se donor technology and sets the stage for future work focused on the biological activity and beneficial applications of H2Se and related bioinorganic RSeS.


Asunto(s)
Compuestos de Selenio/metabolismo , Células HeLa , Humanos , Hidrólisis , Estructura Molecular , Especies Reactivas de Oxígeno/metabolismo , Compuestos de Selenio/química
2.
Micromachines (Basel) ; 11(6)2020 May 28.
Artículo en Inglés | MEDLINE | ID: mdl-32481670

RESUMEN

Retinal implant devices are becoming an increasingly realizable way to improve the vision of patients blinded by photoreceptor degeneration. As an electrode material that can improve restored visual acuity, carbon nanotubes (CNTs) excel due to their nanoscale topography, flexibility, surface chemistry, and double-layer capacitance. If vertically aligned carbon nanotubes (VACNTs) are biocompatible with retinal neurons and mechanically robust, they can further improve visual acuity-most notably in subretinal implants-because they can be patterned into high-aspect-ratio, micrometer-size electrodes. We investigated the role of an aluminum (Al) underlayer beneath an iron (Fe) catalyst layer used in the growth of VACNTs by chemical vapor deposition (CVD). In particular, we cultured dissociated retinal cells for three days in vitro (DIV) on unfunctionalized and oxygen plasma functionalized VACNTs grown from a Fe catalyst (Fe and Fe + Pl preparations, where Pl signifies the plasma functionalization) and an Fe catalyst with an Al underlayer (Al/Fe and Al/Fe + Pl preparations). The addition of the Al layer increased the mechanical integrity of the VACNT interface and enhanced retinal neurite outgrowth over the Fe preparation. Unexpectedly, the extent of neurite outgrowth was significantly greater in the Al/Fe than in the Al/Fe+Pl preparation, suggesting plasma functionalization can negatively impact biocompatibility for some VACNT preparations. Additionally, we show our VACNT growth process for the Al/Fe preparation can support neurite outgrowth for up to 7 DIV. By demonstrating the retinal neuron biocompatibility, mechanical integrity, and pattern control of our VACNTs, this work offers VACNT electrodes as a solution for improving the restored visual acuity provided by modern retinal implants.

3.
Nature ; 449(7165): 1033-6, 2007 Oct 25.
Artículo en Inglés | MEDLINE | ID: mdl-17960240

RESUMEN

The ability of mass spectrometry to generate intact biomolecular ions efficiently in the gas phase has led to its widespread application in metabolomics, proteomics, biological imaging, biomarker discovery and clinical assays (namely neonatal screens). Matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization have been at the forefront of these developments. However, matrix application complicates the use of MALDI for cellular, tissue, biofluid and microarray analysis and can limit the spatial resolution because of the matrix crystal size (typically more than 10 mum), sensitivity and detection of small compounds (less than 500 Da). Secondary-ion mass spectrometry has extremely high lateral resolution (100 nm) and has found biological applications although the energetic desorption/ionization is a limitation owing to molecular fragmentation. Here we introduce nanostructure-initiator mass spectrometry (NIMS), a tool for spatially defined mass analysis. NIMS uses 'initiator' molecules trapped in nanostructured surfaces or 'clathrates' to release and ionize intact molecules adsorbed on the surface. This surface responds to both ion and laser irradiation. The lateral resolution (ion-NIMS about 150 nm), sensitivity, matrix-free and reduced fragmentation of NIMS allows direct characterization of peptide microarrays, direct mass analysis of single cells, tissue imaging, and direct characterization of blood and urine.


Asunto(s)
Espectrometría de Masas/instrumentación , Espectrometría de Masas/métodos , Nanoestructuras , Adsorción , Animales , Análisis Químico de la Sangre , Neoplasias de la Mama/química , Neoplasias de la Mama/patología , Línea Celular Tumoral , Embrión de Mamíferos/química , Iones/química , Rayos Láser , Ratones , Microscopía Electrónica de Rastreo , Nanoestructuras/química , Análisis por Matrices de Proteínas , Sensibilidad y Especificidad , Orina/química
4.
J Biomater Sci Polym Ed ; 16(12): 1463-83, 2005.
Artículo en Inglés | MEDLINE | ID: mdl-16370058

RESUMEN

The object of this work was to produce polyurethanes with greater affinity for albumin (Alb) and improved hemocompatibility by introduction of carboxyl-terminated alkyl side-chains that better mimic fatty acids, in contrast to methyl terminated alkyl side-chains used previously. Synthesis of poly(ether urethane)s (PEUs) with long alkyl side-chains via a multi-step solution addition polymerization is described. The synthesis is based upon the polymerization of a diisocyanate pre-polymer with various chain extenders and reaction with Br-terminated compound in the final stage. The side-chains had terminal methyl or carboxylic groups, and were attached either directly to the polymer backbone or to an oligo(ethylene glycol) spacer. The bulk structure of the PEUs was confirmed by 1H-NMR and the surface polymer structure was characterized by ToF-SIMS. The influence of the incorporated C16-alkyl, C16-carboxyalkyl and oxyethylene-C16-carboxyalkyl side-chains attached to the polymer backbone on fibrinogen (Fg) and Alb adsorption from blood plasma, and Fg adsorption from buffer solutions and binary mixtures with Alb was measured. Incorporation of C16-alkyl or C16-carboxyalkyl side-chains into PEUs caused relatively small changes in Fg and Alb adsorption. PEUs with oxyethylene-C16-carboxyalkyl side-chains exhibited the lowest Fg adsorption and the highest Alb adsorption among all the tested polymers.


Asunto(s)
Biomimética , Ácidos Grasos/química , Poliuretanos/química , Poliuretanos/síntesis química , Proteínas/farmacocinética , Adsorción , Animales , Tampones (Química) , Bovinos , Fibrinógeno/química , Fibrinógeno/farmacocinética , Humanos , Radioisótopos de Yodo , Isocianatos/química , Resonancia Magnética Nuclear Biomolecular , Proteínas/química , Albúmina Sérica/química , Albúmina Sérica/farmacocinética , Soluciones , Espectrometría de Masa por Ionización de Electrospray
5.
J Biomed Mater Res A ; 64(1): 38-47, 2003 Jan 01.
Artículo en Inglés | MEDLINE | ID: mdl-12483694

RESUMEN

Interpenetrating polymer networks (IPNs) of poly(acrylamide-co-ethylene glycol/acrylic acid) (p(AAm-co-EG/AAc) applied to model surfaces prevent protein adsorption and cell adhesion. Subsequently, IPN surfaces functionalized with the RGD cell-binding domain from rat bone sialoprotein (BSP) modulated bone cell adhesion, proliferation, and matrix mineralization. The objective of this study was to utilize the same biomimetic modification strategy to produce functionally similar p(AAm-co-EG/AAc) IPNs on clinically relevant titanium surfaces. Contact angle goniometry and X-ray photoelectron spectroscopy (XPS) data were consistent with the presence of the intended surface modifications. Cellular response was gauged by challenging the surfaces with primary rat calvarial osteoblast (RCO) surfaces in serum-containing media. IPN modified titanium and negative control (RGE-IPN) surfaces inhibit cell adhesion and proliferation, while RGD-modified IPNs on titanium supported osteoblast attachment and spreading. Furthermore, the latter surfaces supported significant mineralization despite exhibiting lower levels of proliferation than positive control surfaces. These results suggest that with the appropriate optimization, this approach may be practical for surface engineering of osseous implants.


Asunto(s)
Osteoblastos/citología , Péptidos/química , Polímeros/química , Titanio/química , Secuencia de Aminoácidos , Animales , Adhesión Celular , División Celular , Células Cultivadas , Microanálisis por Sonda Electrónica , Técnicas In Vitro , Microscopía Fluorescente , Datos de Secuencia Molecular , Ratas , Propiedades de Superficie
6.
J Pharm Sci ; 91(6): 1474-87, 2002 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-12115847

RESUMEN

Recombinant human interferon-gamma (rhIFN-gamma) was lyophilized or spray-lyophilized in 9.5% trehalose, +/- 0.12% polysorbate 20 in 10 mM potassium phosphate, pH 7.5. We measured recovery of soluble protein after spraying, freeze-thawing, and drying and reconstitution. Infrared spectroscopy showed rhIFN-gamma secondary structure to be native-like in all dried powders. Powders were characterized using electron spectroscopy for chemical analysis, time-of-flight secondary ion mass spectroscopy, X-ray diffraction, and gas adsorption isotherms. rhIFN-gamma adsorbed at air/liquid interfaces during spraying, and to ice/liquid interfaces during lyophilization. The concentration of rhIFN-gamma at ice/liquid interfaces was approximately one-fourth that adsorbed at air/liquid interfaces. Addition of 0.12% polysorbate 20 reduced the concentration of rhIFN-gamma at both interfaces. Time-of-flight secondary ion mass spectroscopy detected polysorbate 20 on surfaces of lyophilized powders. Lyophilized samples dried more slowly but reconstituted more quickly than spray-lyophilized samples. rhIFN-gamma aggregated after nebulization, but aggregation decreased in 0.12% polysorbate 20. Addition of 0.12% polysorbate 20 reduced protein surface adsorption and decreased but did not completely prevent aggregation. Insignificant aggregation occurred after exposure to ice/liquid interfaces, but subsequent drying and reconstitution caused aggregation. The majority of the aggregation is due to adsorption at air-liquid and solid-air interfaces formed during spray-lyophilization or lyophilization.


Asunto(s)
Interferón gamma/química , Tensoactivos/química , Química Farmacéutica , Liofilización , Humanos , Polisorbatos/química , Polvos , Proteínas Recombinantes/química
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