Palmitoyl Hexapeptide-12 (Biopeptide EL)
Cosmetic-Grade
Palmitoyl Hexapeptide-12, marketed under the trade name Biopeptide EL, is a synthetic lipopeptide consisting of a palmitoyl (C16 fatty acid) chain conjugated to the hexapeptide sequence Val-Gly-Val-Ala-Pro-Gly (VGVAPG). This sequence is derived from a highly conserved repeat motif found in human tropoelastin — the soluble precursor of mature elastin fibers. The VGVAPG hexamer is one of the most studied elastin-derived peptides in extracellular matrix biology, first characterized by Senior, Griffin, and Mecham in the 1980s as a chemotactic and bioactive fragment released during elastin turnover. The rationale for Palmitoyl Hexapeptide-12 in skincare is distinct from collagen-targeting peptides like Matrixyl or GHK-Cu. While most anti-aging peptides focus on collagen synthesis, skin aging also involves progressive degradation of the elastic fiber network — the structural system responsible for skin recoil, resilience, and the ability to return to shape after deformation. Elastin loss manifests clinically as sagging, loss of firmness, and reduced skin resilience, particularly in photoaged skin where UV-induced elastase activity accelerates elastic fiber degradation. By supplying an exogenous elastin fragment signal, Palmitoyl Hexapeptide-12 aims to stimulate fibroblasts to produce new tropoelastin and support elastic fiber assembly. The bioactive VGVAPG sequence interacts with the 67-kDa elastin-binding protein (EBP), a splice variant of beta-galactosidase that serves as a cell-surface receptor for elastin and elastin-derived peptides. Binding to EBP activates intracellular signaling cascades including ERK1/2 MAP kinase and PI3K/Akt pathways, which upregulate tropoelastin gene expression and promote fibroblast proliferation. The palmitoyl group enhances skin penetration by increasing lipophilicity, allowing the peptide to traverse the stratum corneum barrier. Once in the dermis, skin esterases cleave the palmitoyl moiety to release the bioactive VGVAPG fragment. In vitro studies, primarily from ingredient manufacturers, have demonstrated that Palmitoyl Hexapeptide-12 can increase tropoelastin synthesis in cultured human dermal fibroblasts. However, the clinical evidence base is limited compared to collagen-targeting peptides. Published independent peer-reviewed clinical trials are sparse, and most efficacy data comes from manufacturer-sponsored studies presented at cosmetic science conferences. The ingredient is typically used at concentrations of 2–5 ppm in finished formulations, often combined with collagen-stimulating peptides (such as Matrixyl 3000 or palmitoyl pentapeptide-4) for a comprehensive approach to both collagen and elastin components of dermal aging.
Specifications
| Origin / Manufacturer | Synthetic (biomimetic lipopeptide) |
| Regulatory Status | INCI-listedEU CosIng registered |
| Active Components | Palmitoyl Hexapeptide-12 |
| Storage | Room temperature in finished formulations; raw material store at 2–8°C |
| Shelf Life | Per formulation specifications; raw material 24 months refrigerated |
| Form Factor | Solution (cosmetic raw material) or in finished serums, creams, and eye treatments |
Frequently Asked Questions
Sources & References
Every clinical claim on this page traces to a primary peer-reviewed source.
- 1Senior RM, Griffin GL, Mecham RP. Chemotactic activity of elastin-derived peptides. Journal of Clinical Investigation. 1980;66(4):859-862. doi:10.1172/JCI109926 PMID:6903189
- 2Senior RM, Griffin GL, Mecham RP, Wrenn DS, Prasad KU, Urry DW. Val-Gly-Val-Ala-Pro-Gly, a repeating peptide in elastin, is chemotactic for fibroblasts and monocytes. Journal of Cell Biology. 1984;99(3):870-874. doi:10.1083/jcb.99.3.870 PMID:6144103
- 3Mecham RP, Hinek A, Entwistle R, Wrenn DS, Griffin GL, Senior RM. Elastin binds to a multifunctional 67-kilodalton peripheral membrane protein. Biochemistry. 1989;28(9):3716-3722. doi:10.1021/bi00435a014 PMID:2546579
- 4Hinek A, Rabinovitch M, Keeley F, Okamura-Oho Y, Callahan J. The 67-kD elastin/laminin-binding protein is related to an enzymatically inactive, alternatively spliced form of beta-galactosidase. Journal of Clinical Investigation. 1993;91(3):1198-1205. doi:10.1172/JCI116279 PMID:8450047
- 5Robinet A, Fahem A, Cauchard JH, et al.. Elastin-derived peptides enhance angiogenesis by promoting endothelial cell migration and tubulogenesis through upregulation of MT1-MMP. Journal of Cell Science. 2005;118(Pt 2):343-356. doi:10.1242/jcs.01613 PMID:15632108
- 6Lintner K, Peschard O. Biologically active peptides: from a laboratory bench curiosity to a functional skin care product. International Journal of Cosmetic Science. 2000;22(3):207-218. doi:10.1046/j.1467-2494.2000.00019.x PMID:18503474
- 7Duca L, Floquet N, Aïx AE, Ramont L, Debelle L. Elastin as a matrikine. Critical Reviews in Oncology/Hematology. 2004;49(3):235-244. doi:10.1016/j.critrevonc.2003.09.007 PMID:15036262
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