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Use of an Octapeptide–Guanidiniocarbonylpyrrole Conjugate for the Formation of a Supramolecular β‐Helix that Self‐Assembles into pH‐Responsive Fibers
Author(s) -
Li Mao,
Radić Stojković Marijana,
Ehlers Martin,
Zellermann Elio,
Piantanida Ivo,
Schmuck Carsten
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201605522
Subject(s) - supramolecular chemistry , helix (gastropod) , vesicle , conjugate , chemistry , peptide , triple helix , crystallography , bilayer , biophysics , self assembly , lipid bilayer , transmembrane domain , transmembrane protein , membrane , stereochemistry , receptor , biochemistry , organic chemistry , crystal structure , biology , ecology , mathematical analysis , mathematics , snail
Peptides that adopt β‐helix structures are predominantly found in transmembrane protein domains or in the lipid bilayer of vesicles. Constructing a β‐helix structure in pure water has been considered difficult without the addition of membrane mimics. Herein, we report such an example; peptide 1 self‐assembles into a supramolecular β‐helix in pure water based on charge interactions between the individual peptides. Peptide 1 further showed intriguing transitions from small particles to helical fibers in a time‐dependent process. The fibers can be switched to vesicles by changing the pH value.