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The proteinaceous components of Ap silk proteins, namely fibroin and sericin may represent an alternative over mulberry <jats:italic>Bombyx mori<\/jats:italic> silk proteins. In fact, the silk fibroin (SF) of Ap is rich in Arginyl\u2010Glycyl\u2010Aspartic acid (RGD) peptides, which facilitate the adhesion and proliferation of various cell types. The possibility of processing Ap silk proteins into different distinct 2D\u2010 and 3D\u2010based matrices is described in earlier studies, such as membranes, nanofibers, scaffolds, and micro\/nanoparticles, contributing to a different rate of degradation, mechanical properties, and biological performance useful for various biomedical applications. This review summarizes the current advances and developments on nonmulberry Chinese oak tasar silk protein (fibroin and sericin)\u2010based biomaterials and their potential uses in tissue engineering, regenerative medicine, and therapeutic delivery strategies.<\/jats:p>","DOI":"10.1002\/mabi.201800252","type":"journal-article","created":{"date-parts":[[2018,10,8]],"date-time":"2018-10-08T07:45:38Z","timestamp":1538984738000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":41,"title":["Chinese Oak Tasar Silkworm <i>Antheraea pernyi<\/i> Silk Proteins: Current Strategies and Future Perspectives for Biomedical Applications"],"prefix":"10.1002","volume":"19","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4268-9419","authenticated-orcid":false,"given":"Simone S.","family":"Silva","sequence":"first","affiliation":[{"name":"3B's Research Group I3Bs\u2014Research Institute on Biomaterials Biodegradables and Biomimetics University 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