Phosphatidylserine-selective conformational change of α-helix peptide, Td3717, and its ability to transfect cancer cells

Shinichi Kuriyama, Kanako Nishimura, Yasushi Taguchi, Kazutoshi Yanagibashi, Yoshiki Katayama, Takuro Niidome

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

A synthetic peptide, Td3717, showed selective affinity for anionic phospholipids, phosphatidylserine and phosphatidylglycerol, and formed an amphiphilic α-helical structure. This specificity originated not only from electrostatic interactions, but also from the primary amino acid sequence and overall structure of the peptide.

Original languageEnglish
Pages (from-to)684-685
Number of pages2
JournalChemistry Letters
Volume38
Issue number7
DOIs
Publication statusPublished - Jul 20 2009

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Phosphatidylserines
Cells
Phosphatidylglycerols
Peptides
Coulomb interactions
Phospholipids
Amino Acids

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

Cite this

Phosphatidylserine-selective conformational change of α-helix peptide, Td3717, and its ability to transfect cancer cells. / Kuriyama, Shinichi; Nishimura, Kanako; Taguchi, Yasushi; Yanagibashi, Kazutoshi; Katayama, Yoshiki; Niidome, Takuro.

In: Chemistry Letters, Vol. 38, No. 7, 20.07.2009, p. 684-685.

Research output: Contribution to journalArticle

Kuriyama, Shinichi ; Nishimura, Kanako ; Taguchi, Yasushi ; Yanagibashi, Kazutoshi ; Katayama, Yoshiki ; Niidome, Takuro. / Phosphatidylserine-selective conformational change of α-helix peptide, Td3717, and its ability to transfect cancer cells. In: Chemistry Letters. 2009 ; Vol. 38, No. 7. pp. 684-685.
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AU - Niidome, Takuro

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