| Literature DB >> 23385091 |
Ren-Quan Ruan1, Shan-Shan Wang, Chang-Li Wang, Li Zhang, Yun-Jiao Zhang, Wei Zhou, Wei-Ping Ding, Pei-Pei Jin, Peng-Fei Wei, Na Man, Long-Ping Wen.
Abstract
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.Entities:
Mesh:
Substances:
Year: 2013 PMID: 23385091 DOI: 10.1016/j.ejmech.2012.12.054
Source DB: PubMed Journal: Eur J Med Chem ISSN: 0223-5234 Impact factor: 6.514