Self-assembly of hydrophobic and amphiphilic dodecapeptides was studied in solution and phospholipid bilayer membrane. A hydrophobic dodecapeptide, which took a partial helical conformation, aggregated at the membrane surface, whilst an amphiphilic dodecapeptide was dispersed at the membrane surface. One or two chains of hydrophobic or amphiphilic dodecapeptide were connected to a cyclic octapeptide. Single chain of dodecapeptide when connected to a cyclic peptide increased the helix content significantly. All the peptides having the cyclic peptide formed a more regular assembly in phospholipid membrane than the dodecapeptide without the cyclic peptide. The hydrophobic dodecapeptide connected to a cyclic octapeptide associated in the membrane with parallel orientation to the bilayer normal. 2 α-Bundle structure at the membrane surface was constructed when two chains of amphiphilic dodecapeptide were connected to a cyclic octapeptide. Cyclic peptide is shown to be a useful template compound for architecture of peptide self-assembly systems.
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