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Modulating the Nucleated Self-Assembly of Tri-?(3) -Peptides Using Cucurbit[n]urils.

ABSTRACT: The modulation of the hierarchical nucleated self-assembly of tri-?(3) -peptides has been studied. ?(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-?(3) -peptides were arrested. Given the limited size of the CB[7] cavity, only one aromatic ?(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.

SUBMITTER: Satav T

PROVIDER: S-EPMC6680354 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature

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Modulating the Nucleated Self-Assembly of Tri-β(3) -Peptides Using Cucurbit[n]urils.

Satav Tushar T Korevaar Peter P de Greef Tom F A TF Huskens Jurriaan J Jonkheijm Pascal P

Chemistry (Weinheim an der Bergstrasse, Germany) 20160729 36

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-as ...[more]

PMID: 27434777

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