Abstract

AbstractCollagen is widely used in the development of new functional materials due to its high structural stability, good biocompatibility, and excellent hydrophilicity, but the collagen protein denatures easily, which makes its thermal stability and mechanical strength difficult to reach some of the parameters required in the application. To solve this, protein crosslinking is an effective way to better use collagen. In this paper, we compared the thermal stability and morphological stability of three kinds of sulfonated calixarenes crosslinked collagen before and after the treatment. The results showed that sulfonated calixarenes could significantly improve the thermal stability and morphological stability of dermal collagen. The reinforcing and toughening mechanism of the sulfonated calixarenes was revealed by scanning electron microscopy (SEM), infrared spectroscopy (FT‐IR), attenuated total reflection‐Fourier transform infrared spectroscopy (ATR‐FTIR), ultraviolet–visible–near‐infrared (UV–vis–NIR) spectrometer, X‐ray diffraction detection (XRD), atomic force microscopy (AFM), and circular dichroism (CD) detection. The results showed that sulfonated calixarenes were evenly distributed in collagen fibers and formed hydrogen bonds or electrovalent bonds with amino groups, peptide groups, or amide groups in collagen to improve the thermal stability of the collagen. Three kinds of sulfonated calixarenes enter collagen fiber to support the collagen, increase the three‐dimensional weave angle of collagen, and improve the physical and mechanical properties of collagen, thereby toughening and enhancing the collagen. Based on the above studies, the reinforcing and toughening mechanism of the sulfonated calixarenes crosslinked collagen was established. Confirmed the existence of hydrogen bonds between the three sulfonated calixarenes and collagen, and the nonchemical bond energy of the system was proportional to the molecular size of sulfonated calixarenes.

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