| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1394351 | European Journal of Medicinal Chemistry | 2013 | 5 Pages |
Peptide chaperon TD1 was discovered to facilitate several proteins' transdermal delivery via topical co-administration. To design a practical, safe system for advanced transdermal peptide, a novel method was carried out. Human epidermal growth factor (hEGF) was selected as the model biological agent and a fusion protein: TD1-hEGF was designed. Study showed that TD1-hEGF not only had the similar bioactivity with native hEGF, but also possessed considerable higher transdermal ability than hEGF and a co-administration of TD1 and hEGF. These results provided convincing evidence for the advantages of TD1-hEGF in cosmetic and medical applications. Moreover, the fusion pattern between the cargoes and TD1 offered a new approach to facilitate other hydrophilic drugs' transdermal delivery for therapeutic application.
Graphical abstractA fusion protein TD1-hEGF was designed. TD1-hEGF delivery and TD1 mixed hEGF delivery were compared. Notably, fusion-delivery got high transdermal efficiency than mix-delivery in vitro.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► We design an effectively biological transdermal system for hEGF delivery from intact skin. ► Peptide chaperon is much more appropriate for fusion protein administration. ► It can provide a superior therapeutic administration approach for hydrophilic biological agent in clinical treatments. ► The glycine–serine linker is also compatible to our transdermal system.
