期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 55, 期 10, 页码 3387-3392出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201510611
关键词
biomimetic hosts; carbohydrates; molecular recognition; receptors; supramolecular chemistry
资金
- Engineering and Physical Sciences Research Council [EP/I028501/1]
- Bristol Chemical Synthesis Doctoral Training Centre [EP/G036764/1]
- Wellcome Trust [099185/Z/12/Z]
- Augustinus Fonden
- Oticon Fonden
- Lundbeck Foundation
- COST Action [CM1005]
- Secretaria General de Universidades, Investigacion y Tecnologia (Junta de Andalucia)
- Wellcome Trust
- Danish Ministry of Science, Innovation and Higher Education [DFF-4181-00206]
- Engineering and Physical Sciences Research Council [1114107, EP/I028501/1, EP/K035746/1, EP/L011999/1, EP/K03927X/1] Funding Source: researchfish
- EPSRC [EP/K035746/1, EP/K03927X/1, EP/I028501/1, EP/L011999/1] Funding Source: UKRI
The combination of a pyrenyl tetraamine with an isophthaloyl spacer has led to two new water-soluble carbohydrate receptors (synthetic lectins). Both systems show outstanding affinities for derivatives of N-acetylglucosamine (GlcNAc) in aqueous solution. One receptor binds the methyl glycoside GlcNAc--OMe with K-a approximate to 20000m(-1), whereas the other one binds an O-GlcNAcylated peptide with K-a approximate to 70000m(-1). These values substantially exceed those usually measured for GlcNAc-binding lectins. Slow exchange on the NMR timescale enabled structural determinations for several complexes. As expected, the carbohydrate units are sandwiched between the pyrenes, with the alkoxy and NHAc groups emerging at the sides. The high affinity of the GlcNAcyl-peptide complex can be explained by extra-cavity interactions, raising the possibility of a family of complementary receptors for O-GlcNAc in different contexts.
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