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Protein nanocoatings on synthetic polymeric nanofibrous membranes designed as carriers for skin cells

M. Bacakova, J. Pajorova, D. Stranska, D. Hadraba, F. Lopot, T. Riedel, E. Brynda, M. Zaloudkova, L. Bacakova,

. 2017 ; 12 (-) : 1143-1160. [pub] 20170209

Jazyk angličtina Země Nový Zéland

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc17023274

Protein-coated resorbable synthetic polymeric nanofibrous membranes are promising for the fabrication of advanced skin substitutes. We fabricated electrospun polylactic acid and poly(lactide-co-glycolic acid) nanofibrous membranes and coated them with fibrin or collagen I. Fibronectin was attached to a fibrin or collagen nanocoating, in order further to enhance the cell adhesion and spreading. Fibrin regularly formed a coating around individual nanofibers in the membranes, and also formed a thin noncontinuous nanofibrous mesh on top of the membranes. Collagen also coated most of the fibers of the membrane and randomly created a soft gel on the membrane surface. Fibronectin predominantly adsorbed onto a thin fibrin mesh or a collagen gel, and formed a thin nanofibrous structure. Fibrin nanocoating greatly improved the attachment, spreading, and proliferation of human dermal fibroblasts, whereas collagen nanocoating had a positive influence on the behavior of human HaCaT keratinocytes. In addition, fibrin stimulated the fibroblasts to synthesize fibronectin and to deposit it as an extracellular matrix. Fibrin coating also showed a tendency to improve the ultimate tensile strength of the nanofibrous membranes. Fibronectin attached to fibrin or to a collagen coating further enhanced the adhesion, spreading, and proliferation of both cell types.

Citace poskytuje Crossref.org

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$a Protein-coated resorbable synthetic polymeric nanofibrous membranes are promising for the fabrication of advanced skin substitutes. We fabricated electrospun polylactic acid and poly(lactide-co-glycolic acid) nanofibrous membranes and coated them with fibrin or collagen I. Fibronectin was attached to a fibrin or collagen nanocoating, in order further to enhance the cell adhesion and spreading. Fibrin regularly formed a coating around individual nanofibers in the membranes, and also formed a thin noncontinuous nanofibrous mesh on top of the membranes. Collagen also coated most of the fibers of the membrane and randomly created a soft gel on the membrane surface. Fibronectin predominantly adsorbed onto a thin fibrin mesh or a collagen gel, and formed a thin nanofibrous structure. Fibrin nanocoating greatly improved the attachment, spreading, and proliferation of human dermal fibroblasts, whereas collagen nanocoating had a positive influence on the behavior of human HaCaT keratinocytes. In addition, fibrin stimulated the fibroblasts to synthesize fibronectin and to deposit it as an extracellular matrix. Fibrin coating also showed a tendency to improve the ultimate tensile strength of the nanofibrous membranes. Fibronectin attached to fibrin or to a collagen coating further enhanced the adhesion, spreading, and proliferation of both cell types.
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$a Pajorova, Julia $u Department of Biomaterials and Tissue Engineering, Institute of Physiology, Czech Academy of Sciences; Second Faculty of Medicine, Charles University, Prague.
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$a Stranska, Denisa $u InStar Technologies, Liberec.
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$a Hadraba, Daniel $u Department of Biomaterials and Tissue Engineering, Institute of Physiology, Czech Academy of Sciences; Department of Anatomy and Biomechanics, Faculty of Physical Education and Sport, Charles University.
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$a Lopot, Frantisek $u Department of Anatomy and Biomechanics, Faculty of Physical Education and Sport, Charles University.
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$a Riedel, Tomas $u Department of Chemistry and Physics of Surfaces and Biointerfaces, Institute of Macromolecular Chemistry.
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$a Brynda, Eduard $u Department of Chemistry and Physics of Surfaces and Biointerfaces, Institute of Macromolecular Chemistry.
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$a Zaloudkova, Margit $u Department of Composites and Carbon Materials, Institute of Rock Structure and Mechanics, Czech Academy of Sciences, Prague, Czech Republic.
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