11 research outputs found
Immunocompatibility evaluation of hydrogel-coated polyimide implants for applications in regenerative medicine
Surface modification of polyimide sheets for regenerative medicine applications
In the present work, two strategies were elaborated to surface-functionalize implantable polyimide sheets. In the first methodology, cross-linkable vinyl groups were introduced on the polyimide surface using aminopropylmethacrylamide. In the second approach, arc:active succinimidyl ester was introduced on the surface of PI. Using the former approach, the aim is to apply a vinyl functionalized biopolymer coating. In the latter approach, any amine containing biopolymer can be immobilized. The foils developed were characterized in depth using a variety of characterization techniques. including atomic force rnicroscopy, static contact angle measurements, and X-ray photoelectron spectroscopy. The results indicated that both modification strategies were successful. The subcutaneous implantation in mice indicated that both modification strategies resulted in biocompatible materials, inducing only limited cellular infiltration to the surrounding tissue
The structure-dependent toxicity, pharmacokinetics and anti-tumour activity of HPMA copolymer conjugates in the treatment of solid tumours and leukaemia
Chimera of IL‑2 Linked to Light Chain of anti-IL‑2 mAb Mimics IL-2/anti-IL‑2 mAb Complexes Both Structurally and Functionally
IL-2/anti-IL-2 mAb immunocomplexes
were described to have dramatically
higher activity than free IL-2 <i>in vivo</i>. We designed
protein chimera consisting of IL-2 linked to light chain of anti-IL-2
mAb S4B6 through flexible oligopeptide spacer (Gly<sub>4</sub>Ser)<sub>3</sub>. This protein chimera mimics the structure of IL-2/S4B6 mAb
immunocomplexes but eliminates general disadvantages of immunocomplexes
like possible excess of either IL-2 or anti-IL-2 mAb and their dissociation
to antibody and IL-2 at low concentrations. This novel kind of protein
chimera is characterized by an intramolecular interaction between
IL-2 and binding site of S4B6 mAb similarly as in IL-2/S4B6 mAb immunocomplexes.
Our protein chimera has biological activity comparable to IL-2/S4B6
mAb immunocomplexes <i>in vitro</i>, as shown by stimulation
of proliferation of purified and activated OT-I CD8<sup>+</sup> T
cells. The protein chimera exerts higher stimulatory activity to drive
expansion of purified CFSE-labeled OT-I CD8<sup>+</sup> T cells activated
by an injection of a low dose of SIINFEKL peptide than IL-2/S4B6 mAb
immunocomplexes <i>in vivo</i>