Secondary structures and cell-penetrating abilities of arginine-rich peptide foldamers View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Makoto Oba, Yu Nagano, Takuma Kato, Masakazu Tanaka

ABSTRACT

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-disubstituted α-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. More... »

PAGES

1349

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-018-38063-8

DOI

http://dx.doi.org/10.1038/s41598-018-38063-8

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1111911529

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30718681


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