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Modulating the Nucleated Self‐Assembly of Tri‐β 3 ‐Peptides Using Cucurbit[ n ]urils
Author(s) -
Satav Tushar,
Korevaar Peter,
de Greef Tom F. A.,
Huskens Jurriaan,
Jonkheijm Pascal
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201602896
Subject(s) - supramolecular chemistry , self assembly , chemistry , linker , tyrosine , aromatic amino acids , amino acid , stereochemistry , crystallography , biochemistry , organic chemistry , crystal structure , computer science , operating system
The modulation of the hierarchical nucleated self‐assembly of tri‐β 3 ‐peptides has been studied. β 3 ‐Tyrosine provided a handle to control the assembly process through host‐guest interactions with CB[7] and CB[8]. By varying the cavity size from CB[7] to CB[8] distinct phases of assembling tri‐β 3 ‐peptides were arrested. Given the limited size of the CB[7] cavity, only one aromatic β 3 ‐tyrosine can be simultaneously hosted and, hence, CB[7] was primarily acting as an inhibitor of self‐assembly. In strong contrast, the larger CB[8] can form a ternary complex with two aromatic amino acids and hence CB[8] was acting primarily as cross‐linker of multiple fibers and promoting the formation of larger aggregates. General insights on modulating supramolecular assembly can lead to new ways to introduce functionality in supramolecular polymers.