Abstract
The potential of naturally occurring substances as a source of biomedical materials is well-recognised and is being increasingly exploited. Silk fibroin membranes derived from Bombyx mori silk cocoons exemplify this, for example as substrata for the growth of ocular cells with the aim of generating biomaterial-cell constructs for tissue engineering. This study investigated the transport properties of selected silk fibroin membranes under conditions that allowed equilibrium hydration of the membranes to be maintained. The behaviour of natural fibroin membranes was compared with fibroin membranes that have been chemically modified with poly(ethylene glycol). The permeation of the smaller hydrated sodium ion was higher than that of the hydrated calcium ion for all three ethanol treated membranes investigated. The PEG and HRP-modified C membrane, which had the highest water content at 59.6 ± 1.5% exhibited the highest permeation of the three membranes at 95.7 ± 2.8 × 10–8 cm2 s−1 compared with 17.9 ± 0.9 × 10–8 cm2 s−1 and 8.7 ± 1.7 × 10–8 cm2 s−1 for membranes A and B respectively for the NaCl permeant. Poly(ethylene glycol) was used to increase permeability while exploiting the crosslinking capabilities of horseradish peroxidase to increase the compressive strength of the membrane. Importantly, we have established that the permeation behaviour of water-soluble permeants with hydrated radii in the sub-nanometer range is analogous to that of conventional hydrogel polymers.
Highlights
Fibroin is the main proteinaceous constituent of silk threads made by larvae of the silk moth Bombyx mori, generally, to make webs or cocoons
We have established that the permeation behaviour of water-soluble permeants with hydrated radii in the sub-nanometer range is analogous to that of conventional hydrogel polymers
Structural analysis The secondary structure of the silk fibroin membranes was investigated by infrared spectroscopy, in particular the ‘amide I’ region in the Fourier-transform infrared (FTIR)-attenuated total reflectance (ATR) spectrum (1600–1700 cm−1) which reflects conformational transitions induced in silk fibroin during preparative stages
Summary
Fibroin is the main proteinaceous constituent of silk threads made by larvae of the silk moth Bombyx mori, generally, to make webs or cocoons. A natural polypeptidic composite, it belongs to the group of fibrous proteins characterised by a recurrent sequence of amino acids This leads to a homogeneous secondary structure, a property which responsible for the exceptional functional performance of the silk thread, critical for biomedical applications [1,2,3,4,5]. Silk fibroin membranes have been shown to possess appropriate physico-chemical properties and biocompatibility for a wide range of tissue engineering and biomedical applications including drug delivery and use as implantable devices. Membranes exploiting the use of silk fibroin derived from Bombyx mori are used currently as substrata for the growth of ocular cells with the aim of generating biomaterial-cell constructs of therapeutic significance [3, 6,7,8,9,10,11,12,13]
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