Preparation and characterization of β-cyclodextrin/cimetidine inclusion complexes and interaction mechanism with bovine serum albumin: Multispectrum and molecular dynamics simulation.

Abstract

Cimetidine (CMT) is a first-line for the clinical treatment of peptic ulcers; however, its hydrophobic characteristics and limited half-life limit its further development. β-cyclodextrin (β-CD) served as the host molecule in the synthesis of β-CD/CMT inclusion complexes (ICs). Investigations were conducted on the structure, physicochemical properties, in vitro release behavior of ICs, and interaction with bovine serum albumin (BSA). The findings indicated that β-CD improved the water solubility of CMT, augmented its photo- and thermal stability, delayed its rapid release during the stomach phase, and elevated its bioaccessibility (69.21% → 79.24%). Furthermore, the inclusion of β-CD augmented the binding affinity of CMT to BSA (Kb = 3.32 × 105 → 2.64 × 106 M-1) and enhanced the disruption of BSA's secondary structure. It also mitigated the suppressive influence of CMT on BSA esterase-like activity. Molecular dynamics simulations demonstrated that β-CD enhanced the overall conformational stability of the CMT-BSA complex and promoted formation of more intermolecular hydrogen bonds.

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