Glucosyl-Beta-Cyclodextrin

Dong Q, et al. Journal of Molecular Liquids, 2017, 241, 926-933.

Glucosyl-beta-cyclodextrin (G-β-CD) was employed as a host compound to prepare a water-soluble inclusion complex with neohesperidin dihydrochalcone (NHDC) using an ultrasonic-assisted technique. In the experimental procedure, ethanol–water mixtures (50:50, v/v) containing 10% (w/w) NHDC were combined with 10% (w/w) G-β-CD solutions in varying mass ratios (10–30 g). The mixtures were subjected to ultrasonic treatment at powers ranging from 120 to 360 W and reaction durations between 0.5 and 4 hours in a 25 °C water bath. Following sonication, the mixtures were stored at 0 °C for 24 hours to facilitate complex formation. Precipitated complexes were separated by centrifugation at 5972g for 10 minutes, then dried at 60 °C for 12 hours. Under optimal conditions, the inclusion complex achieved a high NHDC payload of 278 mg/g with an inclusion efficiency of 74.6%, yielding 35–40 g of dried product.

Yoshikiyo K, et al. Journal of Molecular Structure, 2008, 888(1-3), 375-378.

Glucosyl-β-cyclodextrin (G1-β-CD) was demonstrated to significantly accelerate the hydrogen–deuterium (H–D) exchange reaction of peptide hydrogen atoms in lysozyme under deuterated aqueous conditions at elevated temperatures. FT-IR spectroscopy was employed to monitor the exchange kinetics by evaluating the absorbance ratio of the amide II and amide I' bands. At 55 °C, the H–D exchange rate constant of lysozyme doubled in the presence of G1-β-CD compared to the control, whereas no enhancement was observed at 45 °C. In contrast, methyl α-d-glucopyranoside (MG), a non-inclusion analogue, decelerated the exchange rate, underscoring the importance of the inclusion ability of G1-β-CD in facilitating protein conformational changes. The enhancement in exchange rate suggests that G1-β-CD induces partial unfolding or structural rearrangement of lysozyme, thereby exposing peptide bonds to the solvent. The experimental procedure included preparing fully deuterated G1-β-CD through repeated freeze-drying in D₂O, followed by formulation of lysozyme solutions containing either G1-β-CD or MG at glucopyranosyl-equivalent concentrations. This case highlights the functional application of glucosyl-β-cyclodextrin as a molecular chaperone-like additive that promotes peptide bond accessibility in proteins, offering utility in protein structural studies and dynamic analyses through H–D exchange techniques.