Identification and characterization of sericin5 reveals non-cocoon silk sericin components with high β-sheet content and adhesive strength

Abstract

Sericins are glue proteins on the surface of silk fibers. Four sericins have been characterized in silkworm, namely sericin1 (Ser1), sericin2 (Ser2), sericin3 (Ser3), and sericin4 (Ser4). In this study, we report a novel sericin, sericin5 (Ser5), which exists only in non-cocoon silk. We describe the sequence, exon-intron structure, and translation products of Ser5 in Bombyx mori. The Ser5 gene is approximately 22-kb long and comprises 16 exons. Ser5 protein has a size of 260 kDa, as determined by SDS-PAGE, western blot, and LC-MS/MS. Immunofluorescence analysis revealed that Ser5 co-localizes with Ser1 in the sericin layer. The expression pattern of Ser5 was detected at the transcriptional and translational levels. We systematically analyzed and compared the amino acid composition, repeat regions, and hydrophilicity of silkworm sericins. Morphological observations showed that non-cocoon silk had more sericin than cocoon silk. Circular dichroism spectra revealed that non-cocoon silk sericin contained more β-sheet structures than cocoon silk sericin. In addition, we found that the hydrophilicity and adhesive strength of native sericin increases gradually from the inner layer to the outer layer. This research enhances our understanding of various sericins from cocoon silk and non-cocoon silk with regard to their expression patterns, hydrophilicity, secondary structure and adhesive performances. Statement of significanceSericin is a natural biomaterial with diverse biological properties, which has long been used as tissue engineering and biomedical applications. However, the composition and distribution of sericins in different kinds of silk are still uncertain, and the properties difference between sericins have not yet been reported. Our study makes a significant contribution to the literature as it identifies the sequence, composition, hydrophilicity and adhesive property of sericins. Moreover, it provides key insights into the structure-function and function-distribution relationships associated with sericins. We believe that this study will arouse the interest to the readership of your journal as it identifies the new complete sequence of sericin and revealed the composition and properties of sericin, thus highlighting their future potentials applications in both the biomaterial and technical fields.