Accelerated Transacylation of Unactivated Phenyl Esters at Physiological pH with β-Cycloaltramine

The recently reported novel cyclodextrin, β-cycloaltramine, exhibits a 5.3 × 10 4 fold acceleration (compared to buffer) in transacylation of unactivated phenyl esters at physiological pH and follows saturation kinetics similar to enzymes. This acceleration is attributed to the change of the nucleop...

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Veröffentlicht in:Supramolecular chemistry 1996-12, Vol.8 (1), p.5-8
Hauptverfasser: Groaning, Michael D., D'souza, Valerian T.
Format: Artikel
Sprache:eng
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Zusammenfassung:The recently reported novel cyclodextrin, β-cycloaltramine, exhibits a 5.3 × 10 4 fold acceleration (compared to buffer) in transacylation of unactivated phenyl esters at physiological pH and follows saturation kinetics similar to enzymes. This acceleration is attributed to the change of the nucleophile and better binding of the substrate by this novel flexible host.
ISSN:1061-0278
1029-0478
DOI:10.1080/10610279608233961