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Burjassot, Spain

Torres-Giner S.,Novel Materials and Nanotechnology Group | Gimeno-Alcaniz J.V.,Cell Culture Laboratory | Ocio M.J.,Novel Materials and Nanotechnology Group | Ocio M.J.,University of Valencia | Lagaron J.M.,Novel Materials and Nanotechnology Group
Journal of Applied Polymer Science | Year: 2011

Bone tissue interfacial scaffolds, which encourage cell growth, are critical determinants for clinical success after implant surgery. Over the years, a number of resorbable configurations have emerged for bone cell support and growth, but only a few have demonstrated clinical efficacy. Polymer coatings produced by electrospinning are regarded as very promising bone interfaces because of the ultrathin-scaled dimensions of its physical structure. In this study, the morphology, composition, thermal properties, and cell growth viability of a number of polylactide-based systems containing different binary and ternary formulations of this biomaterial with collagen and commercial hydroxyapatite nanoparticles were characterized. The best performance in terms of biocompatibility was obtained for the tricomponent system in which the submicron fibers were further subjected to uniaxial orientation process during formation. The in vitro proliferation of the cells, which harbored on these ultrathin-structured mats, was examined by means of a metabolic activity indicator and ensured by means of scanning electron microscopy, and cell anchorage was checked by fluorescent optical microscopy. Finally, the optimum tricomponent material was successfully sterilized for the first time by gamma radiation without noticeable losses in cell-seeding capacity. © 2011 Wiley Periodicals, Inc. Source

Perotti N.,Cell Culture Laboratory | Etcheverrigaray M.,Cell Culture Laboratory | Kratje R.,Cell Culture Laboratory | Oggero M.,Cell Culture Laboratory
Protein Expression and Purification | Year: 2013

A 7-mer hGM-CSF-derived linear epitope (APARSPS) is herein described as a novel and small tag taking into account its particular binding affinity in native conditions that could be easily modified by increasing or lowering the ionic strength. Thus, a 3.4 or 3.8-fold binding increment was observed in high NaCl concentration when the tag was fused to IFN-α2b or when the peptide was in its native environment, respectively. The high salt concentration increased the affinity of the binding interaction and improved the APARSPS epitope binding to the paratope allowing one to design an immunoaffinity chromatography purification step in which the high ionic strength was useful to adsorb the fusion protein to the immunoaffinity matrix and the low ionic strength at pH 9 was valuable to desorb it (a 470-fold purification with a 94%-purity was attained in only one step). Also, this short tag did not affect the functionality of the fusion protein and it was able to be detected both in the natural molecule (hGM-CSF) as in the tagged one with the same high detection limit: 273 pg of each protein. © 2013 Elsevier Inc. All rights reserved. Source

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