Molecular Sensors and Ion Detection (21)Luminescence and Fluorescent Materials (11)Electrospun Nanofibers in Biomedical Applications (10)Analytical Chemistry and Chromatography (8)Supramolecular Self-Assembly in Materials (7)
In studies to date, meshes based on extracellular matrix (ECM) have been extensively used in clinical applications. Unfortunately, little is known about the function of the immunogenic residual, absorbable profile during the tissue repair process. Moreover, there needs to be a recognized preclinical animal model to investigate the safety and efficacy of extracellular matrix meshes. Herein, we designed and fabricated a kind of SIS mesh followed by a scanned electron micrograph characterization and tested α-Gal antigen clearance rate and DNA residual. In order to prove the biocompatibility of the SIS mesh, cell viability, chemotaxis assay and local tissue reaction were assessed by MTT and RTCA cytotoxicity test in vitro as well as implantation and degradation experiments in vivo. Furthermore, we developed a stable preclinical animal model in the porcine ventral hernia repair investigation, which using laparoscopic plus open hybridization method to evaluate tissue adhesion, explant mechanical performance, and histologic analysis after mesh implantation. More importantly, we established a semi-quantitative scoring system to examine the ECM degradation, tissue remodeling and regeneration in the modified porcine surgical hernia model for the first time. Our results highlight the application prospect of the improved porcine ventral hernia model for the safety and efficacy investigation of hernia repair meshes.
International journal of biological macromolecules •
Raffinose family oligosaccharides (RFOs) in food are the main factors causing flatulence in Irritable Bowel Syndrome (IBS) patients and the development of effective approaches for reducing food-derived RFOs is of paramount importance. In this study, polyvinyl alcohol (PVA)-chitosan (CS)-glycidyl methacrylate (GMA) immobilized α-galactosidase was prepared by the directional freezing-assisted salting-out technique, aimed to hydrolyze RFOs. SEM, FTIR, XPS, fluorescence and UV characterization results demonstrated that α-galactosidase was successfully cross-linked in the PVA-CS-GMA hydrogels, forming a distinct porous stable network through the covalent bond between the enzyme and the carrier. Mechanical performance and swelling capacity analysis illustrated that α-gal @ PVA-CS-GMA not only had suitable strength and toughness for longer durability, but also exhibited high water content and swelling capacity for better retention of catalytic activity. The enzymatic properties of α-gal @ PVA-CS-GMA showed an improved Km value, pH and temperature tolerance range, anti-enzymatic inhibitor (melibiose) activity compared to the free α-galactosidase and its reusability was at least 12 times with prolonged storage stability. Finally, it was successfully applied in the hydrolysis of RFOs in soybeans. These findings provide a new strategy for the development of α-galactosidase immobilization system to biological transform the RFOs components in the food for diet intervention of IBS.
The widely used rotavirus (RV) vaccine, Rotateq, contained reassortment strains of human and bovine G1/2/3/4P[5] RVs. The functional and structural features of bovine G1P[5] VP8* were investigated. Bovine G1P[5] VP8* was identified to interact with sialic acids and sialic acid-containing glycans. In addition, P[5] VP8* recognized α-Gal histo-blood group antigens (HBGAs). Bovine G1P[5] VP8* did not hemagglutinate the tested red blood cells. The crystal structure of P[5] VP8* was determined at 1.7 Å. Structural superimposition revealed that P[5] VP8* was most close to human P[8] VP8*, while much further to VP8*s of porcine P[7] and rhesus P[3]. Sequence alignment showed that amino acids of the putative glycan binding site in P[5] VP8* were different to those in P[3]/P[7] VP8*s, indicating that P[5] VP8* may interact with glycans using different mechanism. This study provided more understanding of P[5] RV infection and the interactions of RV VP8* and glycans.