Inspired by marine mussel adhesive proteins, polymers with catechol side groups have been extensively explored in industrial and academic research. Here, Pluronic L-31 alcoholate ions were used as the initiator to prepare a series of polypeptide-Pluronic-polypeptide triblock copolymers via ring-opening polymerization of l-DOPA-N-carboxyanhydride (DOPA-NCA), l-arginine-NCA (Arg-NCA), l-cysteine-NCA (Cys-NCA), and ε-N-acryloyl lysine-NCA (Ac-Lys-NCA). These copolymers demonstrated good biodegradability, biocompatibility, and thermoresponsive properties. Adhesion tests using porcine skin and bone as adherends demonstrated lap-shear adhesion strengths up to 106 kPa and tensile adhesion strengths up to 675 kPa. The antibleeding activity and tissue adhesive ability were evaluated using a rat model. These polypeptide-Pluronic copolymer glues showed superior hemostatic properties and superior effects in wound healing and osteotomy gaps. Complete healing of skin incisions and remodeling of osteotomy gaps were observed in all rats after 14 and 60 days, respectively. These copolymers have potential uses as tissue adhesives, antibleeding, and tissue engineering materials.
In thyroid carcinomas, NIS and TSHR mRNA levels were lower but the proteins were overexpressed. The NIS protein mainly locates in the cytoplasm, which therefore lacks the ability of transporting and absorbing iodine in patients with thyroid carcinoma. In addition, there was no correlation between NIS and TSHR in thyroid cancer, which may explain why, even after TSH stimulation, 10-20% of these malignant tumors are unable to concentrate enough radioiodine for effective therapy.
ABSTRACT. Aptamers that recognize the IgG Fc region are of great interest because of their wide application as an immunology probing tool, for diagnostics, and as affinity agents for antibody purification. We developed a target replacement strategy as a modification of conventional Systematic Evolution of Ligands by EXponential enrichment (SELEX) in order to efficiently select and identify novel DNA aptamers against the Fc region of mouse IgG. In this new approach, multiple IgG subclasses (IgG1, IgG2a, mouse IgG Fc, and anti-HBs IgG) were sequentially used to select aptamers in one continuous SELEX. After 8 rounds of selection, the aptamers were analyzed using dot blot and an electrophoretic mobility shift assay, which showed universal binding capability to different IgG subclasses. Secondary structure analysis of the aptamers indicated that the stem-loop structure of the aptamers play an important role in binding to the common site in different mouse IgG subclasses. This demonstrated the feasibility of using multiple target replacement SELEX for the selection of aptamers. This target replacement strategy is also expected to be useful for selecting aptamers that bind common regions of molecules other than antibodies.
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