As the three-dimensional (3D) architecture of porcine acellular dermal matrix (pADM) mimics the biological characteristics of a native extracellular matrix (ECM), it has been extensively utilized as a tissue scaffold. In this study, a novel pADM-derived micro-and nano electrospun collagen membrane (PDEC) was successfully prepared by the electrospinning technique, using porcine acellular dermal matrix (pADM) as the raw material and 1,1,1,3,3,3-hexafluoro-2-propanol (HIFP) as the solvent, and was characterized by scanning electron microscopy (SEM) analysis. In contrast, another collagen-derived electrospun collagen (CDEC) was also fabricated using pure porcine collagen as the raw material. The structure and composition of the PDEC and CDEC were measured by Fourier transform infrared (FTIR) spectroscopy, SDS-PAGE gel electrophoresis, specific intrinsic viscosity and atomic force microscopy (AFM). The results indicate that the structural integrity of the PDEC is almost maintained and only a small amount of the PDEC was destroyed into gelatin, while almost all of the CDEC was degraded. Moreover, the results of circular dichroism (CD) analysis also demonstrate that the PDEC possesses a higher content of a-helix structure but less b-turn structure. Additionally, the results from ultrasensitive differential scanning calorimetry (US-DSC) and XRD analysis also suggest that the thermal stability and crystallization of the PDEC have little differences compared to collagen. Furthermore, the mechanical properties of the PDEC are significantly enhanced compared to those of the CDEC. Above all, the results obtained in the MTT study indicate that the PDEC has almost the same good biological activity, in terms of cytotoxicity, as natural porcine collagen, and this activity is obviously superior to that of the CDEC. In conclusion, our study provides a new pADM-derived electrospun collagen in which the triple helical structure has seldom been damaged and thus it can be applied as a novel electrospun collagen scaffold for tissue engineering.
Native collagen fibrils (CF) were successfully extracted from bovine tendons using two different methods: modified acid-solubilized extraction for A-CF and pepsin-aided method for P-CF. The yields of A-CF and P-CF were up to 64.91% (±1.07% SD) and 56.78% (±1.22% SD) (dry weight basis), respectively. The analyses of both amino acid composition and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed that A-CF and P-CF were type I collagen fibrils. Both A-CF and P-CF retained the intact crystallinity and integrity of type I collagen’s natural structure by FTIR spectra, circular dichroism spectroscopy (CD) and X-ray diffraction detection. The aggregation structures of A-CF and P-CF were displayed by UV–Vis. However, A-CF showed more intact aggregation structure than P-CF. Microstructure and D-periodicities of A-CF and P-CF were observed (SEM and TEM). The diameters of A-CF and P-CF are about 386 and 282 nm, respectively. Although both A-CF and P-CF were theoretically concordant with the Schmitt hypothesis, A-CF was of evener thickness and higher integrity in terms of aggregation structure than P-CF. Modified acid-solubilized method provides a potential non-enzyme alternative to extract native collagen fibrils with uniform thickness and integral aggregation structure.
As a vital component of wearable electronics, flexible strain sensors have drawn vast attention due to their capabilities in capturing postures and monitoring various human activities. However, most emerging strain...
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