sericin
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Sericin is a protein created by Bombyx mori (silkworms) in the production of silk. Silk is a fibre produced by the silkworm in production of its cocoon. It consists mainly of two proteins, fibroin and sericin. Silk consists of 70–80% fibroin and 20–30% sericin; fibroin being the structural center of the silk, and sericin being the gum coating the fibres and allowing them to stick to each other.
Key facts
- Nonhuman protein.Name
- Sericin 3
- Nonhuman protein.Symbol
- ser3
- Nonhuman protein.Organism
- Bombyx mori
- Nonhuman protein.UniProt
- A8CEQ1
via Wikipedia infobox
Research
1,337 papers- Sericin: A Versatile Protein Biopolymer with Therapeutic Significance.Current pharmaceutical design · 2020
- Melatonin/Sericin Wound Healing Patches: Implications for Melanoma Therapy.International journal of molecular sciences · 2024
- Silk sericin as building blocks of bioactive materials for advanced therapeutics.Journal of controlled release : official journal of the Controlled Release Society · 2023
- Silk Sericin in Dermatological Diseases: From Preclinical Studies to Future Clinical Applications.Macromolecular bioscience · 2025
- Silk Sericin Protein Materials: Characteristics and Applications in Food-Sector Industries.International journal of molecular sciences · 2023
via PubMed
~3 min read
Article
4 sectionsContents
- Structure
- Applications
- See also
- References
Sericin is a protein created by Bombyx mori (silkworms) in the production of silk. Silk is a fibre produced by the silkworm in production of its cocoon. It consists mainly of two proteins, fibroin and sericin. Silk consists of 70–80% fibroin and 20–30% sericin; fibroin being the structural center of the silk, and sericin being the gum coating the fibres and allowing them to stick to each other.
== Structure == Sericin is composed of 18 different amino acids, of which 32% is serine. The secondary structure is usually a random coil, but it can also be easily converted into a β-sheet conformation, via repeated moisture absorption and mechanical stretching. The serine hydrogen bonds give its glue-like quality. The genes encoding sericin proteins have been sequenced. Its C-terminal part contains many serine-rich repeats.