Silk peptides

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Silk peptides, also known as Silk amino acids (SAAs), are a water-soluble mixture of short to medium chain peptides and glycoproteins derived from hydrolysis of raw silk. They are used as an additive in skin and hair care products due to their high levels of serine which has excellent moisture preservation characteristics. They are used to provide a protective barrier and silky feel to lotions, soaps, personal lubricants, hair and skincare products. Silk peptides are produced by hydrolyzing (or breaking apart) silk proteins into smaller peptide chains. Silk peptides have a lower molecular weight than silk protein powders and are claimed to be moisturizing to skin and hair.

Contents

Composition

Silk is made up of two primary proteins; a fibrous protein known as fibroin, and a sticky protein known as sericin, with the two comprising 70–80% and 20–30% of silk, respectively. The source of these silk amino acids is typically the cocoons of the domestic silk moth, Bombyx mori, although other sources are known. Silk peptides are produced by acid hydrolysis of silk followed by neutralization of excess acid, filtration, and further processing steps to remove salts and other impurities followed by freeze drying. [1] The resultant product contains a mixture of peptides typically between 2 to 20 amino acids in length, with a major component being the 18 amino acid fragment GAGAGSGAGAGSGAGAGS comprising three repeat units of the β‑sheet motif Gly-Ala-Gly-Ala-Gly-Ser derived from the repetitive crystalline domain of silk fibroin protein.

Amino acid proportions

Predominant composition of silk amino acids (by weight*): [2] [ verification needed ]

Applications

Due to its proteinous nature, silk peptide is susceptible to the action of proteolytic enzymes, making it digestible and biocompatible; and because of properties like its gelling ability, moisture retention capacity and skin adhesion, it has numerous medical, pharmaceutical and cosmetic applications. [3] [4] [5] [6] [7]

See also

References

  1. ↑ Oh HJ, Jin H, Lee JY, Lee BY (September 2023). "Silk Peptide Ameliorates Sarcopenia through the Regulation of Akt/mTOR/FoxO3a Signaling Pathways and the Inhibition of Low-Grade Chronic Inflammation in Aged Mice". Cells. 12 (18): 2257. doi: 10.3390/cells12182257 . PMID   37759480.
  2. ↑ Shin S, Park D, Yeon S, Jeon J, Kim TK, Joo S, et al. (2009). "Stamina-Enhancing Effects of Silk Amino Acid Preparations in Mice". Laboratory Animal Research. 25: 127–134. S2CID   83666298.
  3. ↑ Cheng Q, Zhang B, He Y, Lu Q, Kaplan DL (October 2017). "Silk Nanofibers as Robust and Versatile Emulsifiers". ACS Applied Materials & Interfaces. 9 (41): 35693–35700. Bibcode:2017AAMI....935693C. doi:10.1021/acsami.7b13460. PMID   28961401.
  4. ↑ Farokhi M, Mottaghitalab F, Fatahi Y, Khademhosseini A, Kaplan DL (September 2018). "Overview of Silk Fibroin Use in Wound Dressings". Trends in Biotechnology. 36 (9): 907–922. doi:10.1016/j.tibtech.2018.04.004. PMID   29764691.
  5. ↑ Niu J, Yuan M, Liu Y, Wang L, Tang Z, Wang Y, et al. (2022). "Silk peptide-hyaluronic acid based nanogels for the enhancement of the topical administration of curcumin". Frontiers in Chemistry. 10 1028372. Bibcode:2022FrCh...1028372N. doi: 10.3389/fchem.2022.1028372 . PMC   9527322 . PMID   36199664.
  6. ↑ González-Restrepo D, Zuluaga-Vélez A, Orozco LM, Sepúlveda-Arias JC (April 2024). "Silk fibroin-based dressings with antibacterial and anti-inflammatory properties". European Journal of Pharmaceutical Sciences. 195 106710. doi: 10.1016/j.ejps.2024.106710 . PMID   38281552.
  7. ↑ Mota A, Caçador M, Carvalho JP, Tinoco A, da Costa A, Ribeiro A, et al. (October 2025). "Cosmetic Potential of a Structural Protein Copolymer Based on Silk, Elastin, and Keratin". ACS Biomaterials Science & Engineering. 11 (10): 6185–6194. doi:10.1021/acsbiomaterials.5c01233. hdl: 1822/98149 . PMID   40987580.
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