Enzymatic crosslinking of silk sericin through combined use of TGase and the custom peptide

Abstract

Silk sericin (SS) is derived from natural Bombyx mori silk fibers, and it has the unique biological properties like good biocompatibility and low immunogenicity. However, pure SS material exhibits poor mechanical properties and high water solubility, which greatly reduces the formability of SS material and limits its wide range of applications. In this study, a transglutaminase (TGase) was combinedly used with two custom peptides of GQGEGQG (p-Q) and KKKK (p-K), containing exogenous glutamine and lysine residues, respectively, for facilitating the enzymatic crosslinking of sericin proteins. The efficacy of enzymatic incubation was assessed by the means of SDS-PAGE, size exclusion chromatography chromatogram, and determination of the quantitative changes in amino groups. Properties of the obtained SS membranes based on different treatments were also examined. The results revealed that incubating of SS with TGase and glutamine-containing peptide led to a noticeable increase in the molecular weight compared with others. TGase-mediated treatments had detectable impact on the conformational structures of SS, the obtained formability and mechanical property for the TGase/p-Q treated SS membrane were evidently improved compared to others. The suggestive alternative, based on the combination use of TGase and p-Q has the potential applications for preparation of the sericin-based biomaterials.