Supramolecular Control over Split‐Luciferase Complementation

Abstract: Supramolecular split‐enzyme complementation restores enzymatic activity and allows for on–off switching. Split‐luciferase fragment pairs were provided with an N‐terminal FGG sequence and screened for complementation through host‐guest binding to cucurbit[8]uril (Q8). Split‐luciferase heterocomplex formation was induced in a Q8 concentration dependent manner, resulting in a 20‐fold upregulation of luciferase activity. Supramolecular split‐luciferase complementation was fully reversible, as revealed by using two types of Q8 inhibitors. Competition studies with the weak‐binding FGG peptide revealed a 300‐fold enhanced stability for the formation of the ternary heterocomplex compared to binding of two of the same fragments to Q8. Stochiometric binding by the potent inhibitor memantine could be used for repeated cycling of luciferase activation and deactivation in conjunction with Q8, providing a versatile module for in vitro supramolecular signaling networks.

Location
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch

Bibliographic citation
Supramolecular Control over Split‐Luciferase Complementation ; volume:128 ; number:31 ; year:2016 ; pages:9045-9049 ; extent:5
Angewandte Chemie ; 128, Heft 31 (2016), 9045-9049 (gesamt 5)

Creator
Bosmans, Ralph P. G.
Briels, Jeroen M.
Milroy, Lech‐Gustav
de Greef, Tom F. A.
Merkx, Maarten
Brunsveld, Luc

DOI
10.1002/ange.201602807
URN
urn:nbn:de:101:1-2022110106253461755186
Rights
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
15.08.2025, 7:26 AM CEST

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Associated

  • Bosmans, Ralph P. G.
  • Briels, Jeroen M.
  • Milroy, Lech‐Gustav
  • de Greef, Tom F. A.
  • Merkx, Maarten
  • Brunsveld, Luc

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