2016
DOI: 10.1166/jbt.2016.1517
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Electrospun Silk Fibroin/Polycaprolactone Biomimetic Scaffold for Peripheral Nerve Regeneration

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Cited by 6 publications
(3 citation statements)
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“…The nutrients, metabolites, and body fluid transfer through the scaffolds are correlated with the water absorption ability . The scaffold requires a certain degree of hydrophobicity and liquid absorption capacity, which means that scaffolds could not only allow substance exchange in tissue, but also not excessively expand to oppress tissue when materials implanted in the body.…”
Section: Resultsmentioning
confidence: 99%
“…The nutrients, metabolites, and body fluid transfer through the scaffolds are correlated with the water absorption ability . The scaffold requires a certain degree of hydrophobicity and liquid absorption capacity, which means that scaffolds could not only allow substance exchange in tissue, but also not excessively expand to oppress tissue when materials implanted in the body.…”
Section: Resultsmentioning
confidence: 99%
“…Most extracellular proteins such as collagen (which is an abundant ECM protein) have a fibrous structure with typical dimensions in the nanometer or submicrometer scales (50 to 500 nm) . Therefore, the use of electrospun nanofibrous scaffolds for tissue engineering applications has attracted considerable attention due to the straightforward processing ability of a wide range of materials such as poly­(lactic acid) (PLA), poly­(lactic- co -glycolic acid) (PLGA), polycaprolactone (PCL), PLGA/PCL, and synthetic polymers combined with natural collagen, gelatin, alginate, silk, chitin, and chitosan . Additionally, electrospun NFs offer a tunable porosity and a dynamically changing structure over time as the polymeric NFs degrade, allowing the seeded cells to proliferate and produce their own ECM. …”
Section: Introductionmentioning
confidence: 99%
“…This may be related to the change in microstructure of the SF and the content of the β-sheet crystal structure. 42 We thought that the β-sheet structure of SF was non-water-soluble, the structure of α helix/random coil without soaking ethanol was water-soluble. Therefore, the hydrophilicity of rigid β-sheet structure was slightly worse than that of α helix/random coil resulting in the fibers thinning.…”
Section: Resultsmentioning
confidence: 99%