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Effects of an Amphiphilic Peptide on Membrane Order of Phosphatidylcholine by Kiyoshi Mishima; Hitomi Watanabe; Satoshi Kaneko; Toshihiko Ogihara is a Materials Science article available to read on EtoBox.

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Amphiphilic sequences located at N terminal of secretory proteins and integral membrane proteins, the so called signal sequences or topogenic sequences, lead insertion of the following polypeptide segments into biomembranes. We have a lot of knowledge about the sequential structure and the steric conformation, whereas poor knowledge about interaction between the signal sequences and membranes. We studied effects of a synthetic amphiphilic peptide on chain orientational order of lipid membranes by the optical birefringence method at high peptide concentrations. The synthetic peptide is modeled on the signal sequences. The peptide with 20 amino acid residues has a hydrophobic region (Ala(7), Leu(7) and Trp) with hydrophilic amino acids (Lys(6)) at the end. The hydrophobic region forms a-helix structure. Multilamellar vesicles of synthetic dimyristoyl-(DMPC) and dipalmitoyl-phosphatidylcholines (DPPC), and of natural egg yolk phosphatidylcholine (Egg-PC) were prepared as lipid model membranes. It was observed that interference light due to the membrane birefringence considerably decreased by addition of the peptide for both DMPC and DPPC multilamellar bilayers, but did not change for

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Author

Kiyoshi Mishima; Hitomi Watanabe; Satoshi Kaneko; Toshihiko Ogihara

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0927-7765)

Published

2002

Language

EN

Field

Materials Science (Physical Sciences)