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The six amino acid antimicrobial peptide bLF cin 6 penetrates cells and delivers siRNA
Author(s) -
Fang Bing,
Guo Hui Y,
Zhang Ming,
Jiang Lu,
Ren Fa Z
Publication year - 2013
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12093
Subject(s) - peptide , antimicrobial , antimicrobial peptides , chemistry , amino acid , microbiology and biotechnology , biochemistry , biology
Cell‐penetrating peptides ( CPP s) are a new class of vectors with high pharmaceutical potential to deliver bioactive cargos into cells. Here, we characterized bLF cin 6 , a six amino acid peptide derived from bovine lactoferricin, as a CPP . Uptake of bLF cin 6 was measured by flow cytometry. The ability to delivery siRNA was analyzed in HeLa cells. bLF cin 6 exhibited concentration‐dependent uptake and intracellular distribution. Below 7.5 μ m , uptake of bLF cin 6 was significantly lower than uptake of TAT ( P < 0.05) because bLF cin 6 has fewer cationic amino acids. Compared to CPP 5 ( RLRWR ) and CPP 6 ( PFVYLI ), bLF cin 6 had a significantly higher internalization ratio above 2.5 μ m because it has two tryptophan residues. Uptake of bLF cin 6 starts with an ionic cell‐surface interaction. It is then rapidly internalized by lipid raft‐dependent macropinocytosis, followed by release from macropinosomes into the cytosol and nucleus. Moreover, bLF cin 6 formed stable electrostatic complexes with si RNA and delivered si RNA into cells, resulting in significant knockout activity at both the mRNA and protein levels. The knockout activity of si RNA delivered by bLF cin 6 was similar to that mediated by TAT , although knockout by bLF cin 6 required a higher molar ratio. In this study, bLF cin 6 was tested for its ability to act as an si RNA ‐delivering CPP .