Premium
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
Abstract 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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom