The interaction mechanisms analysis of shikonin with α-glucosidase by multi-spectroscopic and molecular docking methods

Abstract

This study aimed to investigate the binding mechanism of shikonin with α-glucosidase by multi-spectroscopic and molecular docking technologies. These data suggested that shikonin spontaneously interacted with α-glucosidase primarily through hydrogen bonds (H-bond) and van der Waals forces (vdW), the quenching mechanism was static quenching. At 298 K, the quenching rate constant and binding constant were (1.00 ± 0.06) × 10¹² L mol⁻¹ s⁻¹ and (2.32 ± 0.04) × 10⁴ L mol⁻¹, respectively. Molecular docking analysis also confirmed the results of the spectroscopic method. These results are helpful in understanding the interaction mechanism between shikonin and α-glucosidase.

Keywords:

• Shikonin
• α-glucosidase
• spectroscopy
• interaction mechanism
• type 2 diabetes mellitus
• molecular docking

Disclosure statement

No potential conflict of interest was reported by the author(s).

Author contributions

Dan Liu: Writing-Original Draft Preparation, Investigation. Ye Cheng: Investigation. Yanjun Li: Data Curation. Jingyi Miao: Investigation, Data Curation. Xiangyu Cao: Project administration, Writing - review & editing, Supervision.

Data availability statement

The data are available from the corresponding author upon reasonable request.

Additional information

Funding

This study was supported by the Program for Liaoning Innovative Talents in University (No. LD2020002).