Fabrication of nanofibers from wild varieties of silk such as eri and tasar is very promising for tissue engineering application because of the presence of RGD (arginine-glycine-aspartic acid) ligand and high content of hydrophilic amino acids. In this study, the biodegradation of silk fibroin (SF) nanofibers have been studied in protease XIV solution to analyze the degradation behavior. The present study reveals that the degradation of nanofibrous mat strongly depends on hydrophilic amino acid fragments possessing bulky groups connecting the crystalline portion in nanofibrous structure. The newly found mechanism shows that beta sheet content and percentage of crystal in nanofibers play a major role in addition to hydrophilic fragments in degradation processes. Understanding of this mechanism can optimize the preparation of nanofibers with controlled and flexible degradation behavior without affecting essential bi(o)material properties such as hydrophilicity, mechanical strength, and morphological property. This knowledge would widen the application of silk-based biomaterial for several tissues engineering application.
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