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

被引：24

作者：

Ruan, Ren-quan ^{[1
]}

Wang, Shan-shan ^{[1
]}

Wang, Chang-li ^{[1
]}

Zhang, Li ^{[1
]}

Zhang, Yun-jiao ^{[1
]}

Zhou, Wei ^{[1
]}

Ding, Wei-ping ^{[1
]}

Jin, Pei-pei ^{[1
]}

Wei, Peng-fei ^{[1
]}

Man, Na ^{[1
]}

Wen, Long-ping ^{[1
]}

机构：

[1] Univ Sci & Technol China, Sch Life Sci, Hefei 230026, Peoples R China

来源：

EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY | 2013年 / 62卷

关键词：

Transdermal drug delivery; Human epidermal growth factor; Peptide chaperon; Transdermal peptide; PENETRATION; MIGRATION; PROTEIN; EGF;

D O I：

10.1016/j.ejmech.2012.12.054

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

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. (C) 2013 Elsevier Masson SAS. All rights reserved.

引用

页码：405 / 409

页数：5

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