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Natural and genetically engineered proteins for tissue engineering

Gomes, Sílvia C.; Leonor, I. B.; Mano, J. F.; Reis, R. L.; Kaplan, David

To overcome the limitations of traditionally used autografts, allografts and, to a lesser extent, synthetic materials, there is the need to develop a new generation of scaffolds with adequate mechanical and structural support, control of cell attachment, migration, proliferation and differentiation and with bio-resorbable features. This suite of properties would allow the body to heal itself at the same rate as...


Biological responses to spider silk - antibiotic fusion protein

Gomes, Sílvia C.; Gallego-Llamas, Jabier; Leonor, I. B.; Mano, J. F.; Reis, R. L.; Kaplan, David

The development of a new generation of multifunctional biomaterials is a continual goal for the field of materials science. The in vivo functional behaviour of a new fusion protein that combines the mechanical properties of spider silk with the antimicrobial properties of hepcidin was addressed in this study. This new chimeric protein, termed 6mer + hepcidin, fuses spider dragline consensus sequences (6mer) and...


Spider silk-bone sialoprotein fusion proteins for bone tissue engineering

Gomes, Sílvia C.; Leonor, I. B.; Mano, J. F.; Reis, R. L.; Kaplan, David

The remarkable mechanical characteristics of the spider silk protein major ampullate spidroin protein suggest this polymer as a promising biomaterial to consider for the fabrication of scaffolds for bone regeneration. Herein, a new functionalized spider silk-bone sialoprotein fusion protein was designed, cloned, expressed, purified and the osteogenic activity studied. Bone sialoprotein (BSP) is a multidomain pr...


Antimicrobial functionalized genetically engineered spider silk

Gomes, Sílvia C.; Leonor, I. B.; Mano, J. F.; Reis, R. L.; Kaplan, David

Genetically engineered fusion proteins offer potential as multifunctional biomaterials for medical use. Fusion or chimeric proteins can be formed using recombinant DNA technology by combining nucleotide sequences encoding different peptides or proteins that are otherwise not found together in nature. In the present study, three new fusion proteins were designed, cloned and expressed and assessed for function, b...


AFM study of morphology and mechanical properties of a chimeric 2 spider silk a...

Gomes, Sílvia C.; Numata, Keiji; Leonor, I. B.; Mano, J. F.; Reis, R. L.; Kaplan, David

Atomic force microscopy (AFM) was used to assess a new chimeric protein consisting of a fusion protein of the consensus repeat for Nephila clavipes spider dragline protein and bone sialoprotein (6merþBSP). The elastic modulus of this protein in film form was assessed through force curves, and film surface roughness was also determined. The results showed a significant difference among the elastic modulus of the...


The effects of Anodonta cygnea biological fluids on biomineralization of chitos...

Lopes, Anabela; Lima, Manuel Lopes; Bobos, Iulius; Ferreira, Jorge; Gomes, Sílvia C.; Reis, R. L.; Mano, J. F.; Machado, Jorge

The use of chitosan membranes, a low-cost, biocompatible material with promising capabilities in biomedical applications has already been fairly investigated in other fields with good results. Here, the aim was the in vitro mineralization assays accomplished with the chitosan membranes incubated in the control calcium and phosphate solutions on “Ussing” chambers. Biological fluids from Anodonta cygnea were adde...


Mineralization of chitosan membrane using a double diffusion system for bone re...

Gomes, Sílvia C.; Boulon, M. E.; Oliveira, A. L.; Leonor, I. B.; Mano, J. F.; Reis, R. L.

Chitosan membranes were subjected to a pre-treatment in a double diffusion system, with a calcium solution in one chamber and a phosphate solution in the other chamber. Both chambers were separated by the chitosan membrane and subject to three mineralization periods (5, 10 and 15 minutes). After this pre-treatment the bioactivity of the different calcium phosphate coatings formed was tested for different period...


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    Financiadores do RCAAP

Fundação para a Ciência e a Tecnologia Universidade do Minho   Governo Português Ministério da Educação e Ciência Programa Operacional da Sociedade do Conhecimento União Europeia