Stability Is Not Everything: The Case of the Cyclisation of a Thrombin-Binding Aptamer.
G-quadruplexes
aptamers
click chemistry
cyclization
molecular recognition
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
15 07 2019
15 07 2019
Historique:
received:
23
01
2019
pubmed:
13
3
2019
medline:
22
7
2020
entrez:
13
3
2019
Statut:
ppublish
Résumé
With the aim of developing a new approach to obtain improved aptamers, a cyclic thrombin-binding aptamer (TBA) analogue (cycTBA) has been prepared by exploiting a copper(I)-assisted azide-alkyne cycloaddition. The markedly increased serum resistance and exceptional thermal stability of the G-quadruplex versus TBA were associated with halved thrombin inhibition, which suggested that some flexibility in the TBA structure was necessary for protein recognition.
Identifiants
pubmed: 30860635
doi: 10.1002/cbic.201900045
doi:
Substances chimiques
Aptamers, Nucleotide
0
thrombin aptamer
145563-68-4
Thrombin
EC 3.4.21.5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1789-1794Informations de copyright
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.