Abstract
Design of bundled peptides has become of interest in recent year, because such peptides are useful not only as models of natural proteins but also as functional materials. We previously reported that an amphiphilic α-helical 24 mer peptide 46 showed strong activity toward phospholipid membrane [1]. Bundled peptides, 4α-46 composed of 4 fragments of the 46 chains and 4α-46S in which 24 Ser residues are present instead of the Leu and Ala residues in 4α-4 6, had much stronger membrane perturbation activity than 46 [2]. In the present study, we synthesized more hydrophilic bundled peptides containing 36 Ser residues, [Trp2]and [Trp12]-4α-46 S9, and examined their properties.
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