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Interaction of bundled Ser‐rich amphiphilic peptides with phospholipid membranes
Author(s) -
Yoshida Kazutoshi,
Ohmori Naoya,
Mukai Yasuhiro,
Niidome Takuro,
Hatakeyama Tomomitsu,
Aoyagi Haruhiko
Publication year - 1999
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/(sici)1099-1387(199908)5:8<360::aid-psc208>3.0.co;2-q
Subject(s) - chemistry , vesicle , peptide , membrane , phosphatidylglycerol , amphiphile , phosphatidylcholine , phospholipid , circular dichroism , liposome , biophysics , chromatography , biochemistry , organic chemistry , biology , copolymer , polymer
To investigate properties of hydrophilic bundled peptides and their interactions with phospholipid membranes, bundled peptides named [Trp 2 ]‐ and [Trp 12 ]‐4α‐4 6 S9, which are composed of four fragments of amphiphilic 24‐mer peptide, were designed and synthesized. Tryptophan (Trp) was introduced at the 2nd position from the N‐terminal or at the centre (12th) of the helix to monitor the peptide–lipid interaction. Circular dichroism measurements indicated that the peptides had low α‐helicities in a buffer solution (pH 7.4) and also in the presence of dipalmitoyl‐ dl ‐3‐phosphatidylcholine (DPPC) vesicles. In the presence of DPPC/dipalmitoyl‐ dl ‐3‐phosphatidylglycerol (DPPG) (3:1) vesicles, the measurement could not be taken because of turbidity induced by vesicle aggregation. Both peptides had moderate perturbation activity for both the neutral and acidic vesicles at 25°C. The perturbation patterns at 50°C were much different from those at 25°C and the maximum activity reached 100% at a low peptide concentration. The results of the measurement of membrane fusion activity of peptides showed a similar tendency to that found in the perturbation experiment. A quenching experiment indicated that the Trp 2 and Trp 12 residues in [Trp 2 ]‐ and [Trp 12 ]‐4α‐4 6 S9 were scarcely embedded in neutral lipid membranes. Copyright © 1999 European Peptide Society and John Wiley & Sons, Ltd.