Helical poly(arginine) mimics with superior cell-penetrating and molecular transporting properties

Haoyu Tang; Lichen Yin; Kyung Hoon Kim; Jianjun Cheng

doi:10.1039/c3sc51328a

Helical poly(arginine) mimics with superior cell-penetrating and molecular transporting properties

Haoyu Tang, Lichen Yin, Kyung Hoon Kim, Jianjun Cheng

Research output: Contribution to journal › Article › peer-review

Abstract

Poly(arginine) mimics bearing long hydrophobic side chains adopt a stable helical conformation and exhibit helix-related cell-penetrating properties. Elongating the polypeptide backbone length and increasing side chain hydrophobicity further increase the helicities of poly(arginine) mimics. These helical poly(arginine) mimics show superior cell membrane permeability up to two orders of magnitude higher than that of HIV-TAT peptide and excellent DNA and siRNA delivery efficiencies in various mammalian cells.

Original language	English (US)
Pages (from-to)	3839-3844
Number of pages	6
Journal	Chemical Science
Volume	4
Issue number	10
DOIs	https://doi.org/10.1039/c3sc51328a
State	Published - Aug 26 2013
Externally published	Yes

ASJC Scopus subject areas

General Chemistry

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10.1039/c3sc51328a

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abstract = "Poly(arginine) mimics bearing long hydrophobic side chains adopt a stable helical conformation and exhibit helix-related cell-penetrating properties. Elongating the polypeptide backbone length and increasing side chain hydrophobicity further increase the helicities of poly(arginine) mimics. These helical poly(arginine) mimics show superior cell membrane permeability up to two orders of magnitude higher than that of HIV-TAT peptide and excellent DNA and siRNA delivery efficiencies in various mammalian cells.",

author = "Haoyu Tang and Lichen Yin and Kim, {Kyung Hoon} and Jianjun Cheng",

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AU - Tang, Haoyu

AU - Yin, Lichen

AU - Kim, Kyung Hoon

AU - Cheng, Jianjun

PY - 2013/8/26

Y1 - 2013/8/26

N2 - Poly(arginine) mimics bearing long hydrophobic side chains adopt a stable helical conformation and exhibit helix-related cell-penetrating properties. Elongating the polypeptide backbone length and increasing side chain hydrophobicity further increase the helicities of poly(arginine) mimics. These helical poly(arginine) mimics show superior cell membrane permeability up to two orders of magnitude higher than that of HIV-TAT peptide and excellent DNA and siRNA delivery efficiencies in various mammalian cells.

AB - Poly(arginine) mimics bearing long hydrophobic side chains adopt a stable helical conformation and exhibit helix-related cell-penetrating properties. Elongating the polypeptide backbone length and increasing side chain hydrophobicity further increase the helicities of poly(arginine) mimics. These helical poly(arginine) mimics show superior cell membrane permeability up to two orders of magnitude higher than that of HIV-TAT peptide and excellent DNA and siRNA delivery efficiencies in various mammalian cells.

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Helical poly(arginine) mimics with superior cell-penetrating and molecular transporting properties

Abstract

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