Abstract
Abstract A 26-residue peptide containing six histidine (H) residues showed a pH-dependent interaction with a membrane. At a basic pH, where the H residues were deprotonated, the peptides formed a helical structure and adopted a transmembrane alignment in the lipid vesicles. At an acidic pH, where the H residues were protonated, they exhibited a mixture of β and random forms and were aggregated or dissolved in the aqueous phase.
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