Arginine-rich Peptides
By S. Futaki, T. Suzuki, W. Ohashi, T. Yagami, Shoichiro Tanaka, K. Ueda, Y. Sugiura. Journal of Biological Chemistry, 2001
1,194 citations recorded by the source corpus.
A basic peptide derived from human immunodeficiency virus (HIV)-1 Tat protein (positions 48–60) has been reported to have the ability to translocate through the cell membranes and accumulate in the nucleus, the characteristics of which are utilized for the delivery of exogenous proteins into cells. Based on the fluorescence microscopic observations of mouse macrophage RAW264.7 cells, we found that various arginine-rich peptides have a translocation activity very similar to Tat-(48–60). These included such peptides as the d-amino acid- and arginine-substituted Tat-(48–60), the RNA-binding peptides derived from virus proteins, such as HIV-1 Rev, and flock house virus coat proteins, and the DNA binding segments of leucine zipper proteins, such as cancer-related proteins c-Fos and c-Jun, and the yeast transcription factor GCN4. These segments have no specific primary and secondary structures in common except that they have several arginine residues in the sequences. Moreover, these peptides were able to be internalized even at 4 °C. These results strongly suggested the possible existence of a common internalization mechanism ubiquitous to arginine-rich peptides, which is not explained by a typical endocytosis. Using (Arg) n (n = 4–16) peptides, we also demonstrated that there would be an optimal number of arginine residues (n ∼ 8) for the efficient translocation.
Subfields: Genetics, Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/312a3197d9ace5446e4fccd0177417b93bdd8b88
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Citations in the corpus
- Mechanisms of Cellular Uptake of Cell-Penetrating Peptides (2011, background): “There is evidence for both energy-independent processes and endocytosis in internalization of CPPs. Presently, endocytosis, composed of two steps, endocytotic entry followed by endosomal escape, is believed to be the most common uptake mechanism at low CPP concentrations [2, 9].”
- Twenty years of cell-penetrating peptides: from molecular mechanisms to therapeutics (2009, positive): “The groups of Wender and of Futaki demonstrated that polyarginine sequences (Arg8) were sufficient to drive molecules into cells and proposed that their uptake mechanism involves a bidentate hydrogen-bonding interaction between guanidinium group of arginine residues and phosphate group in the membra”