A Helix‐Stabilized Cell‐Penetrating Peptide as an Intracellular Delivery Tool. Issue 2 (3rd December 2015)

• Record Type: Journal Article
• Authors: Yamashita, Hiroko; Oba, Makoto; Misawa, Takashi; Tanaka, Masakazu; Hattori, Takayuki; Naito, Mikihiko; Kurihara, Masaaki; Demizu, Yosuke
• Is Part Of: Chembiochem. Volume 17:Issue 2(2016)
• Page Start: 137
• Page End: 140
• Publication Date: 2015-12-03
• Subjects: cell-penetrating peptides -- helical structure -- non-proteinogenic amino acids -- plasmid DNA delivery; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201500468
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: Two types of cationic cyclic α, α‐disubstituted α‐amino acids: Api C 2 NH 2 (which possesses a lysine mimic side chain) and Api C2Gu (which possesses an arginine mimic side chain), were developed. These amino acids were incorporated into an arginine‐based peptide sequence [(l ‐Arg‐l ‐Arg‐dAA)3 : dAA=Api C 2 NH 2 or Api C2Gu ], and the relationship between the secondary structures of the resulting peptides and their ability to pass through cell membranes was investigated. The peptide containing Api C2Gu formed a stable α‐helical structure and was more effective at penetrating cells than the nonhelical Arg nonapeptide (R9 ). Furthermore, the peptide was able to deliver plasmid DNA into various types of cells in a highly efficient manner. Abstract : Getting in there : The helix stabilization of arginine‐based oligopeptides has been shown to affect their cellular uptake efficiency. A helix‐stabilized arginine‐rich peptide delivered plasmid DNA into various types of cells in a highly efficient manner, particularly compared to its nonhelical counterpart. This provides insight into the development of intracellular delivery systems.