No abstract

In this work, a nano-in-micro carrier was constructed by loading polymer-lipid hybrid nanoparticles (NPs) into porous and hollow yeast cell wall microparticles (YPs) for macrophage-targeted oral delivery of cabazitaxel (CTX). The YPs, primarily composed of natural β-1,3-d-glucan, can be recognized by the apical membrane receptor, dectin-1, which has a high expression on macrophages and intestinal M cells. By combining electrostatic force-driven self-deposition with solvent hydration/lyophilization methods, the positively charged NPs loaded with CTX or fluorescence probes were efficiently packaged into YPs, as verified by scanning electron microscope (SEM), atomic force mircoscope (AFM), and confocal laser scanning microscopy (CLSM) images. NP-loaded YPs (NYPs) showed a slower in vitro drug release and higher drug stability compared with NPs in a simulated gastrointestinal environment. Biodistribution experiments confirmed a widespread distribution and extended retention time of NYPs in the intestinal tract after oral administration. Importantly, a large amount of NYPs were primarily accumulated and transported in the intestinal Peyer's patches as visualized in distribution and absorption site studies, implying that NYPs were mainly absorbed through the lymphatic pathway. In vitro cell evaluation further demonstrated that NYPs were rapidly and efficiently taken up by macrophages via receptor dectin-1-mediated endocytosis using a mouse macrophage RAW 264.7 cell line. As expected, in the study of in vivo pharmacokinetics, the oral bioavailability of CTX was improved to 32.1% when loaded in NYPs, which is approximately 5.7 times higher than that of the CTX solution, indicating the NYPs are efficient for oral targeted delivery. Hence, this nano-in-micro carrier is believed to become a hopeful alternative strategy for increasing the oral absorption of small molecule drugs.

Electrostatic particle complexes, CPP/TPP/NP, consisting of PEG-modified silica NPs with TPP and CPP, showed satisfactory stability and mucous penetration.

Preparation and applications of monolithic structures containing metal-organic frameworksMetal-organic frameworks are a new category of advanced porous materials with large surface areas and porosities, uniform pore sizes, tunable surface chemistry, and structural diversity. In combination with monoliths, they allow the fine tuning of desired interactions required in a variety of applications. This review article summarizes results of recent studies focused on synthetic strategies enabling incorporation of metal-organic frameworks in monolithic structures. A diverse array of applications including chromatographic separation, solid-phase microextraction, sample enrichment, heterogeneous catalysis, and enzymatic catalysis are also described.

Pretreatment of lignocellulosic biomass with sulfuric acid may leave sulfate groups on its surface that may hinder its biochemical conversion. This study investigates the effects of sulfate groups on cellulase adsorption onto cellulose substrates and the enzymatic hydrolysis of these substrates. Substrates with different sulfate group densities were prepared from H2SO4- and HCl-hydrolyzed and partially and fully desulfated cellulose nanocrystals. Adsorption onto and hydrolysis of the substrates was analyzed by quartz crystal microbalance with dissipation monitoring (QCM-D). The surface roughness of the substrates, measured by atomic force microscopy, increased with decreasing sulfate group density, but their surface accessibilities, measured by QCM-D H2O/D2O exchange experiments, were similar. The adsorption of cellulose binding domains onto sulfated substrates decreased with increasing sulfate group density, but the adsorption of cellulases increased. The rate of hydrolysis of sulfated substrates decreased with increasing sulfate group density. The results indicated an inhibitory effect of sulfate groups on the enzymatic hydrolysis of cellulose, possibly due to nonproductive binding of the cellulases onto the substrates through electrostatic interactions instead of their cellulose binding domains.