Phosphatidylserine-selective Conformational Change of α-Helix Peptide, Td3717, and Its Ability to Transfect Cancer Cells

Phosphatidylserine-selective Conformational Change of α-Helix Peptide, Td3717, and Its Ability to Transfect Cancer Cells

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 overal...

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Veröffentlicht in:Chemistry letters 2009-07, Vol.38 (7), p.684-685
Hauptverfasser: Kuriyama, Shinichi, Nishimura, Kanako, Taguchi, Yasushi, Yanagibashi, Kazutoshi, Katayama, Yoshiki, Niidome, Takuro
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:0366-7022
1348-0715
DOI:10.1246/cl.2009.684