Protein-mediated dethreading of a biotin-functionalised pseudorotaxane - Université de Lille Accéder directement au contenu
Article Dans Une Revue Organic & Biomolecular Chemistry Année : 2014

Protein-mediated dethreading of a biotin-functionalised pseudorotaxane

Résumé

In this article, we describe the synthesis of new biotin-functionalised naphthalene derivatives 3 and 4 and their complexation behaviour with avidin and neutravidin using a range of analytical techniques. We have shown using 2-(4′-hydroxyazobenzene)benzoic acid displacement and ITC experiments, that compounds 3 and 4 have the propensity to form reasonably high-affinity bioconjugates with avidin and neutravidin. We have also demonstrated using 1H NMR, UV-vis and fluorescence spectroscopy that the naphthalene moiety of 3 and 4 facilitates the formation of pseudorotaxane-like structures with 1 in water. We have then investigated the ability of avidin and neutravidin to modulate the complexation between 1 and 3 or 4. UV-vis and fluorescence spectroscopy has shown that in both cases the addition of the protein disrupts complexation between the naphthalene moieties of 3 and 4 with 1.
Fichier principal
Vignette du fichier
c3ob41612g.pdf (873.85 Ko) Télécharger le fichier
Origine : Fichiers éditeurs autorisés sur une archive ouverte
Loading...

Dates et versions

hal-02544680 , version 1 (16-04-2020)

Licence

Paternité

Identifiants

Citer

Stuart T Caldwell, Catherine Maclean, Mathis Riehle, Alan Cooper, Margaret Nutley, et al.. Protein-mediated dethreading of a biotin-functionalised pseudorotaxane. Organic & Biomolecular Chemistry, 2014, Organic & Biomolecular Chemistry, 12, pp.511-516. ⟨10.1039/c3ob41612g⟩. ⟨hal-02544680⟩
27 Consultations
75 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More