Induced helical conformation of ionic polypeptides by phospholipids solubilized in a nonionic surfactant solution

International Journal of Peptide and Protein Research
K Shirahama, J T Yang

Abstract

Phosphatidylcholine that has been solubilized in hexadecylpoly (oxyethylene) ether can induce a coil-to-helix transformation for poly (L-glutamic acid) in neutral solution. Similarly, solubilized phosphatidylserine promotes a helical conformation of poly (L-lysine) at neutral pH through complex formation. The mixed micelles of a phospholipid and a nonionic surfactant are thermodynamically stable and do not separate on standing. The nonionic surfactant here has no effect on the conformation of the two polypeptides.

References

Apr 1, 1977·Biopolymers·Y W Tseng, J T Yang
Jan 20, 1965·Journal of the American Chemical Society·G HOLZWARTH, P DOTY

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Citations

Mar 1, 1990·International Journal of Peptide and Protein Research·A G Appu RaoD J Winzor
Apr 9, 2015·Soft Matter·Brad H JonesErik D Spoerke
Sep 1, 1980·International Journal of Peptide and Protein Research·K Ikeda, J T Yang
Sep 15, 1989·Biophysical Chemistry·K FukushimaR Shimozawa
Aug 31, 1989·Biochimica Et Biophysica Acta·A G RaoJ R Cann
Oct 4, 2005·Biophysical Journal·Helen SjögrenStefan Ulvenlund

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