Abstract
Concentrated collagen hydrolysate (HC10CC), rabbit collagen glue (RCG), and keratin hydrolysate (KH) were investigated in terms of their extraction from mammalian by-products and processing by electrospinning. The electrospun nanofibers were characterized by scanning electron microscopy coupled with the energy dispersive X-ray spectroscopy (SEM/EDS), attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR), differential scanning calorimetry (DSC), and indentation tests. The cytotoxicity of the electrospun nanofibers was conducted on L929 fibroblast cells using MTT and LDH assays and cell morphology observations. The electrospun RCG and KH nanofibers morphology showed an average size of nanofibers ranging between 44 and 410 nm, while the electrospun HC10CC nanofibers exhibited higher sizes. The ATR-FTIR spectra performed both on extracted proteins and electrospun nanofibers showed that the triple helix structure of collagen is partially preserved. The results were in agreement with the circular dichroism analysis for protein extracts. Furthermore, the viscoelastic properties of electrospun KH nanofibers were superior to those of electrospun RCG nanofibers. Based on both in vitro quantitative and qualitative analysis, the electrospun nanofibers were not cytotoxic, inducing a healthy cellular response. The results of new electrospun protein-based nanofibers may be useful for further research on bioactive properties of these nanofibers for tissue engineering.
Highlights
The research on the biocompatible natural polymers processing by electrospinning for biomedical applications has increased in recent years [1,2]
The objectives of this study were (1) to extract and characterize the collagen hydrolysate (HC10), collagen glue (RCG), and keratin hydrolysate (KH) from bovine tanned leather by-products, pickled rabbit skin, and sheepskin wool, respectively; (2) to characterize the protein-based nanofibers obtained by electrospinning for potential biomedical field application; and (3) to demonstrate that the structure of protein-based nanofibers still preserves the secondary collagen structure without being totally affected by the extraction and electrospinning processing conditions
The experiments showed that the concentrated collagen hydrolysate extracted from bovine leather by-products, rabbit skin collagen glue, and keratin hydrolysate from wool waste have the properties required for electrospinning processing
Summary
The research on the biocompatible natural polymers processing by electrospinning for biomedical applications has increased in recent years [1,2]. Nanofibers with different thermoplastic polymers, biomaterials, or active compounds (dyes, drugs, light-sensitive or conductive organics, and piezoelectric materials) [3] can be obtained by electrospinning. Collagen and keratin are the most valuable natural biomaterials due to their chemical versatility and biological performance. They mimic the extracellular matrices (ECM) of tissues and organs, which consist in a complex composite of fibrous proteins such as collagen and fibronectin, glycoproteins, proteoglycans, and soluble proteins (growth factors, bioactive molecules that support cell adhesion and proliferation). Collagen is a natural biopolymer, the most abundant protein in mammals, which is widely used in bone restoration engineering [11], processing of controlled release of drug systems [12], as well as in food [13] and cosmetics [14]
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