An Insight on Silk Protein Sericin: From Processing to Biomedical Application

Abstract

Silks are naturally occurring polymers that have been used clinically as sutures for hundreds of years. It's so for obtained from insects or worms, silk consists of a filament core protein, termed fibroin, and a glue-like coating made up of sericin proteins. An important component of silk has an extended history of being discarded as a waste in the course of silk processing. The cost of sericin for tissue engineering is underestimated and its capability in using as regenerative remedy has simply began to be explored. Its variable amino acid composition and various functional groups confer upon it attractive bioactive proteins, which are particularly interesting for biomedical programs. Because of its antioxidant properties, moisturizing ability, and mitogenic effect on mammalian cells, sericin is beneficial in cell regeneration and tissue engineering. Research shows that keratinocytes and fibroblasts have brought about the improvement of sericin-primarily based biomaterials for skin tissue repair, in particular as wound dressings. Moreover, sericin may be used for bone tissue engineering due to its ability to set off nucleation of bone-like hydroxyapatite. Stable silk sericin biomaterials, as films, sponges, and hydrogels, are obtained by means of cross-linking, ethanol precipitation, or mixing with different polymers. Now a day, sericin may also be used for delivery of drugs due to its chemical reactivity and pH-responsiveness which facilitate the fabrication of nano and microparticles, hydrogels, and conjugated molecules, enhancing the bioactivity of drugs. In this review, we outlined the current headways from extraction of sericin till its physical properties and biomedical applications.

Recent Advances in Silk Sericin/Calcium Phosphate Biomaterials

“…Although some authors mention the potential of sericin/CaP as scaffolds for TE (Takeuchi et al, 2003b;Yang et al, 2014b), an ideal 3D scaffold should not only act as a template for tissue growth and has controlled resorbability, but should also elicit a regenerative effect and present adequate mechanical performance over time (Canillas et al, 2017). As previously mentioned, the last requirement is not fulfilled by using only sericin (Ahsan et al, 2018). Immersion cycles: 5, 10, 15 cycles.…”

“…However, emerging evidence suggests that extracted sericin per se is biocompatible, similarly to silk fibroin or collagen (Chirila et al, 2013;Lamboni et al, 2015). Therefore it has been gaining reputation in the biomedical field with several works showing its potential, as revised elsewhere (Kunz et al, 2016;Ahsan et al, 2018). Thus, the use of sericin/CaP composites not only reduces the inherent environmental impact of sericin disposal but also allows the development of new functional biomaterials.…”

“…Thus, this protein is highly hydrophilic and its molecular weight can range from 20 to 400 kDa (Kunz et al, 2016). Its polar side chains have several functional groups (carboxyl, amine, hydroxyl) responsible for moisturizing and oxidizing properties, allowing the interaction with other compounds through crosslinking, copolymerization or blending to form improved biomaterials (Ahsan et al, 2018). According to the literature, amino acids can highly influence the mineralization process of CaPs.…”

Does sericin pleurodesis increase the basic fibroblastic growth factor and high-sensitive c-reactive protein levels in rat plasma?

“…The predominant amino acid in the structure of the sericin protein is serine amino acid and as such, sericin contains strongly polar side groups, such as hydroxyl, carboxyl, amino groups that enable easy cross-linking, and copolymerization that improves both biocompatibility and biodegradation [13,14]. Sericin has many applications, including as an anti-wrinkle, anti-aging, antioxidant and as an additive to cell culture media, and has a healing effect on wounds [1,2,8,[13][14][15][16]. Sericin has good hydrophilic properties that are widely used in the pharmaceuticals and cosmetic sectors.…”

Identification and applications of neuroactive silk proteins: a narrative review

“…Silkworm, the larva or caterpillar of the domesticated silkmoth (Bombyx mori), commercially viable in the production of silk. Silkworms depend upon the leaves of the mulberry trees as food (Ahsan et al, 2018). Excellent physical properties of silk, such as lightweight, high mechanical strength, and flexibility, make it appropriate to produce new biomaterials with application in tissue repair and drug delivery (Florczak et al, 2014).…”