Transdermal delivery of human epidermal growth factor facilitated by a peptide chaperon

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• 作者：Ren-quan Ruan¹ ; Shan-shan Wang¹ ; Chang-li Wang ; Li Zhang ; Yun-jiao Zhang ; Wei Zhou ; Wei-ping Ding² ; Pei-pei Jin ; Peng-fei Wei ; Na Man ; Long-ping Wen ; ^{lpwen@ustc.edu.cn}
• 关键词：Transdermal drug delivery ; Human epidermal growth factor ; Peptide chaperon ; Transdermal peptide
• 刊名：European Journal of Medicinal Chemistry
• 出版年：2013
• 出版时间：April, 2013
• 年：2013
• 卷：62
• 期：Complete
• 页码：405-409
• 全文大小：663 K

文摘

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.