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

doi:10.1246/cl.2009.684

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 journal › Article › peer-review

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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 language	English
Pages (from-to)	684-685
Number of pages	2
Journal	Chemistry Letters
Volume	38
Issue number	7
DOIs	https://doi.org/10.1246/cl.2009.684
Publication status	Published - 2009

All Science Journal Classification (ASJC) codes

Chemistry(all)

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This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1246/cl.2009.684

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

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.",

author = "Shinichi Kuriyama and Kanako Nishimura and Yasushi Taguchi and Kazutoshi Yanagibashi and Yoshiki Katayama and Takuro Niidome",

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doi = "10.1246/cl.2009.684",

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journal = "Chemistry Letters",

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T1 - Phosphatidylserine-selective conformational change of α-helix peptide, Td3717, and its ability to transfect cancer cells

AU - Kuriyama, Shinichi

AU - Nishimura, Kanako

AU - Taguchi, Yasushi

AU - Yanagibashi, Kazutoshi

AU - Katayama, Yoshiki

AU - Niidome, Takuro

PY - 2009

Y1 - 2009

N2 - 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.

AB - 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.

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DO - 10.1246/cl.2009.684

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JF - Chemistry Letters

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

Abstract

All Science Journal Classification (ASJC) codes

UN SDGs

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