Supramolecular structures have emerged as a promising enzyme mimetic. In this study we focused on the resorcinarene hexamer which is a self assembled capsule that have been studied intensively due to it’s ready availability. The hexameric capsule shows some catalytic features reminiscent of natural enzymes include; substrate selectivity , stabilization of transition state and intermediate through secondary interactions, an inherent Bronsted acidity and it’s ability to act as a hydrogen bond catalyst. Inside the cavity of the capsule reagents are confined in a restricted space in close proximity, such that they react faster . Here in, It was shown how the catalytic activity of the capsule can be modulated in the presence of competitive alkyl ammonium guests in the profile of conversion of tri alkyl phosphite substrate to it’s corresponding di alkyl phosphite product. The profile of the reaction was monitored using GC and NMR spectroscopy.

Supramolecular Catalysis in Confined Nano-space

Elrabei Abubakar Osman, Zina
2022/2023

Abstract

Supramolecular structures have emerged as a promising enzyme mimetic. In this study we focused on the resorcinarene hexamer which is a self assembled capsule that have been studied intensively due to it’s ready availability. The hexameric capsule shows some catalytic features reminiscent of natural enzymes include; substrate selectivity , stabilization of transition state and intermediate through secondary interactions, an inherent Bronsted acidity and it’s ability to act as a hydrogen bond catalyst. Inside the cavity of the capsule reagents are confined in a restricted space in close proximity, such that they react faster . Here in, It was shown how the catalytic activity of the capsule can be modulated in the presence of competitive alkyl ammonium guests in the profile of conversion of tri alkyl phosphite substrate to it’s corresponding di alkyl phosphite product. The profile of the reaction was monitored using GC and NMR spectroscopy.
File in questo prodotto:
File Dimensione Formato  
876031-1242654.pdf

accesso aperto

Tipologia: Altro materiale allegato
Dimensione 1.53 MB
Formato Adobe PDF
1.53 MB Adobe PDF Visualizza/Apri

I documenti in UNITESI sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14247/9607