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Secondary structures and cell-penetrating abilities of arginine-rich peptide foldamers.

ABSTRACT: Foldamers, which are folded oligomers with well-defined conformations, have been recently reported to have a good cell-penetrating ability. ?,?-Disubstituted ?-amino acids are one such promising tool for the design of peptide foldamers. Here, we prepared four types of L-arginine-rich nonapeptides containing L-leucine or ?,?-disubstituted ?-amino acids, and evaluated their secondary structures and cell-penetrating abilities in order to elucidate a correlation between them. Peptides containing ?,?-disubstituted ?-amino acids had similar resistance to protease digestion but showed different secondary structures. Intracellular uptake assays revealed that the helicity of peptides was important for their cell-penetrating abilities. These findings suggested that a peptide foldamer with a stable helical structure could be promising for the design of cell-penetrating peptides.

SUBMITTER: Oba M 

PROVIDER: S-EPMC6362038 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature

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Secondary structures and cell-penetrating abilities of arginine-rich peptide foldamers.

Oba Makoto M   Nagano Yu Y   Kato Takuma T   Tanaka Masakazu M  

Scientific reports 20190204 1

Foldamers, which are folded oligomers with well-defined conformations, have been recently reported to have a good cell-penetrating ability. α,α-Disubstituted α-amino acids are one such promising tool for the design of peptide foldamers. Here, we prepared four types of L-arginine-rich nonapeptides containing L-leucine or α,α-disubstituted α-amino acids, and evaluated their secondary structures and cell-penetrating abilities in order to elucidate a correlation between them. Peptides containing α,α  ...[more]

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