RESUMO
Carrageenans have unique properties in the pharmaceutical and food industries that involve interactions with lipid interfaces, which may be accessed if surface chemistry techniques are employed. The interaction between three different types of carrageenans with dipalmitoylphosphatidylcholine (DPPC) was investigated using Langmuir monolayers as biointerface models. With a combination of data on Surface Pressure-Area Isotherms and Polarization Modulation Infrared Reflection-Absorption Spectroscopy (PM-IRRAS), the effect of different fractions on DPPC monolayers was compared by considering the chemical and structural differences as well as the anticoagulant activity of each fraction. Thus, a model is proposed in which carrageenans can encompass interactions that are maximized due to geometrical adaptations on behalf of the interactions between polysaccharide sulfate groups and lipid polar heads.
Assuntos
1,2-Dipalmitoilfosfatidilcolina/química , Materiais Biocompatíveis/química , Carragenina/farmacologia , Anticoagulantes/farmacologia , Carragenina/química , Força Compressiva/efeitos dos fármacos , Heparina/farmacologia , Espectrofotometria Infravermelho , Propriedades de Superfície , TemperaturaRESUMO
In this paper, we investigate the affinity of palladium nanoparticles, stabilized with glucose oxidase, for fatty acid monolayers at the air-water interface, exploiting the interaction between a planar system and spheroids coming from the aqueous subphase. A decrease of the monolayer collapse pressure in the second cycle of interface compression proved that the presence of the nanoparticles causes destabilization of the monolayer in a mechanism driven by the interpenetration of the enzyme into the bilayer/multilayer structure formed during collapse, which is not immediately reversible after monolayer expansion. Surface pressure and surface potential-area isotherms, as well as infrared spectroscopy [polarization modulation infrared reflection adsorption spectroscopy (PM-IRRAS)] and deposition onto solid plates as Langmuir-Blodgett (LB) films, were employed to construct a model in which the nanoparticle has a high affinity for the hydrophobic core of the structure formed after collapse, which provides a slow desorption rate from the interface after monolayer decompression. This may have important consequences on the interaction between the metallic particles and fatty acid monolayers, which implies the regulation of the multifunctional properties of the hybrid material.
Assuntos
Ácidos Graxos/química , Nanopartículas Metálicas/química , Paládio/química , Adsorção , Ar , Ácidos Graxos/metabolismo , Glucose Oxidase/química , Glucose Oxidase/metabolismo , Paládio/metabolismo , Tamanho da Partícula , Propriedades de Superfície , Água/químicaRESUMO
A major challenge for producing low cost biosensors based on nanostructured films with control of molecular architectures is to preserve the catalytic activity of the immobilized biomolecules. In this study, we show that catalase (HRP) keeps its activity if immobilized in Langmuir-Blodgett (LB) films of dipalmitoyl phosphatidylglycerol (DPPG). The incorporation of catalase into a DPPG monolayer at the air-water interface was demonstrated with surface pressure and surface potential isotherms, in addition to polarization-modulated infrared reflection absorption spectroscopy (PM-IRRAS). According to the PM-IRRAS data, catalase was not denatured upon adsorption on a preformed DPPG monolayer and could be transferred onto a solid substrate. The catalytic activity of catalase in a mixed LB film with DPPG was ca. 13% higher than in solution. The control of molecular architecture and choice of a suitable phospholipid matrix allows catalase-containing LB films to be used in sensing hydrogen peroxide.