1H NMR studies of molecular interaction of D-glucosamine and N-acetyl-D-glucosamine with curcumin and caffeic acid phenethyl ester in DMSO
- Evelin Martínez-Benavidez,
- Analilia Sánchez,
- Zaira Domínguez,
- Magali Salas-Reyes,
- Gustavo Adolfo Castillo-Herrera,
- Clúster Científico y Tecnológico Biomimic®,
- Universidad Veracruzana,
- Centro de Investigacion en Alimentacion y Desarrollo,
- Universidad Anáhuac Mayab,
- Universidad de Sonora
Publication Information
Tipo de resultado
Idioma original
InglésNúmero de artículo
109704Revista (Volumen, Número de Edición)
Carbohydrate Research (Volumen 558)Hitos de publicación
- Publicada - 01/12/2025
Estado de publicación
ISSN
0008-6215ID de publicación externa
- Scopus: 105019069346
Abstract
Chitosan (Cs)-based polymers have been explored as potential drug-delivery systems that could enhance the practical applications of bioactive phenolic (Ph) substances, such as curcumin (CUR) and caffeic acid phenethyl ester (CAPE). In this study, we focused on designing CS-based drug carriers by examining the intermolecular interactions between the polymer components, D-glucosamine (Gn) and N-acetyl-D-glucosamine (AGn), and the target substances CUR and CAPE through 1H NMR titration in dimethyl sulfoxide (DMSO‑d6). The observed changes in chemical shifts indicated that Gn cation (GnH+) forms molecular complexes, whereas AGn does not exhibit any intermolecular interaction. We developed a titration curve for the complexation, which competes with the self-association of GnH+ (Gnz) in DMSO. Least-squares analyses concluded that molecular complex represented as Ph·Gnz (z = 3 or 4) is formed through a reaction between a Gnz aggregate and a Ph molecule. The formation constant, K = [Ph·Gnz]/[Ph][Gnz], falls within the range of 50–300 M−1. The complex is stabilized by intermolecular interactions at multiple sites within the glucosamine aggregate Gnz, although the non-covalent interactions at each binding site are relatively weak. These findings suggest that chitosan can capture CAPE or CUR exclusively at segments composed of adjacent cationic glucosamine units.
