Oligopeptide-CB complexation with switchable binding pathways.
Organic & biomolecular chemistry
Royal Society of Chemistry
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Wu, G., Clarke, D. E., Wu, C., & Scherman, O. (2019). Oligopeptide-CB complexation with switchable binding pathways.. Organic & biomolecular chemistry, 17 (14), 3514-3520. https://doi.org/10.1039/c9ob00592g
Host–guest complexes exhibiting a 1:1 binding stoichiometry need not consist of a single host and guest. A series of oligopeptides, which were previously reported to have abnormally high binding enthalpies were investigated to deduce whether they exist as a 2:2 quaternary or a 1:1 binary complex with cucurbituril (CB). Through a systematic study of the sequence-specific binding pathways of peptide-CB association, a phenylalanine-leucine dipeptide was found to be capable of switching from a 1:1 stoichiometric complex to a 2:1 complex. By studying the differences in size-based diffusion properties of these two binding modes, the presence of a 1:1 pairwise inclusion complex was verified for the regime where CB is in excess. Findings in this study can be utilised to ‘customise’ the precise CB-oligopeptide self-assembly pathway, acting as a useful toolbox in the design of supramolecular systems.
Imidazoles, Oligopeptides, Binding Sites, Molecular Structure, Thermodynamics, Bridged-Ring Compounds
The Leverhulme Trust Marie Curie FP7 ERC EPSRC
Leverhulme Trust (RP2013-SL-008)
European Commission (607602)
European Research Council (240629)
External DOI: https://doi.org/10.1039/c9ob00592g
This record's URL: https://www.repository.cam.ac.uk/handle/1810/290893
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