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Transdermal delivery of proteins mediated by non‐covalently associated arginine‐rich intracellular delivery peptides
Author(s) -
Hou YuWun,
Chan MingHuan,
Hsu HuiRu,
Liu Betty Revon,
Chen ChungPin,
Chen HweiHsien,
Lee HanJung
Publication year - 2007
Publication title -
experimental dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.108
H-Index - 96
eISSN - 1600-0625
pISSN - 0906-6705
DOI - 10.1111/j.1600-0625.2007.00622.x
Subject(s) - internalization , transduction (biophysics) , intracellular , pinocytosis , transdermal , chemistry , microbiology and biotechnology , biochemistry , biology , cell , endocytosis , pharmacology
Plasma membranes of animal cells are generally impermeable to macromolecules. Protein transduction mediated by protein transduction domains (PTDs) covalently cross‐linked to cargoes for cellular internalization has previously been demonstrated. Peptides with PTDs could be an effective way to deliver proteins into living cells or tissues in vitro . In this report, we demonstrate that arginine‐rich intracellular delivery (AID) peptides are able to facilitate the delivery of proteins into animal cells and to penetrate skin tissues rapidly. This cellular internalization and transdermal delivery of proteins is mediated by non‐toxic AID peptides in a non‐fusion protein and non‐conjugation dependent manner. The efficiency of intracellular transport is further increased in the presence of chemical enhancer oleic acid. The mechanism of the AID‐mediated cellular entry may involve macropinocytosis and actin rearrangement. Thus, we confirm that direct delivery of bioactive proteins into living cells and tissues mediated by non‐covalent actions of AID peptides represents a useful strategy in pharmaceutics, therapeutics and cosmetics.