As a major flavonoid polyphenolic compound in the stem of Hibiscus taiwanensis, syringaldehyde (SA) has numerous pharmacological effects. Nevertheless, owing to its less in-depth study, its application is limited. Within this work, the interactions between serum albumin and SA were elucidated by multispectral studies. The results of ultraviolet/visible absorption spectroscopy suggest that the conformation of serum albumin can be altered by binding with SA. Fluorescence spectroscopy indicates that SA forms complexes with serum albumin, quenching its fluorescence. This suggests that the fluorescent residues of serum albumin are situated at or near the binding site. Additionally, FT-IR results confirm that SA alters the secondary structure of BSA, specifically affecting the positions of both amide I and amide II bands. Via the computational biology analyses, it was confirmed that SA binds at the active site of serum albumin and nine residues form hydrophobic interactions. In addition, the cytotoxicity of SA to BRL-3A cells was also studied, and SA had almost no toxicity to the growth of BRL-3A cells. The complex has a higher α-amylase inhibition capacity than SA alone. To sum up, this work reveals that the interaction of SA with BSA induces a conformational alteration in BSA. It also proved that SA inhibits α-amylase more significantly and has great potential in hypoglycemia.
Keywords: Cytotoxicity; Multispectral; Serum albumin; Syringaldehyde.
Copyright © 2023. Published by Elsevier B.V.