Sign in Subscribe
Albumin

Multispectral Techniques Reveal Synergistic Effects of Antihypertensive Drug and Natural Compound on Bovine Serum Albumin

Strategic Insights

— 2 min read

Research published in Spectrochimica Acta Part A has shed light on the synergistic effects of the antihypertensive drug benazepril and the natural compound apigenin on bovine serum albumin (BSA). The study, conducted by researchers at Bohai University, employed multispectral techniques to investigate the interactions between BSA, benazepril, and apigenin. The findings indicate that apigenin exhibits a significantly higher binding affinity to BSA than benazepril, inducing stronger conformational perturbations in the protein.

Key Takeaways:

  • Apigenin shows a higher binding affinity to BSA (K = 1.07 x 10^(-7) M) compared to benazepril (K = 3.96 x 10^(-7) M).
  • Apigenin preferentially occupies Site I of BSA, inducing stronger conformational perturbations in the protein (circular dichroism results show a 6.71 % decrease in α-helix content).
  • The coexistence of benazepril and apigenin with BSA leads to a competitive-allosteric-synergistic mechanism, where apigenin inhibits the benazepril-BSA interaction via competitive binding and allosteric effects.
  • The combined use of benazepril and apigenin reduces the energy transfer efficiency (E decreased from 27.42 % to 11.46 %) and increases the binding distance (r increased from 2.82 nm to 3.37 nm) to BSA.
  • Apigenin induces greater disruption to BSA's secondary structure and overall conformation than benazepril, and their combined use synergistically further destabilizes BSA's secondary structure while enhancing the hydrophobicity of the amino acid microenvironment (fluorescence spectra blueshifted by 3.0 nm).
  • Free sulfhydryl group (SH) assays indicate that both apigenin and benzepril protect free SH, with apigenin being the dominant factor.
  • Esterase activity experiments confirmed that apigenin and benazepril synergistically inhibit BSA function.

Statistics:

  • The binding affinity of apigenin to BSA is 1.07 x 10^(-7) M, compared to 3.96 x 10^(-7) M for benazepril.
  • The decrease in α-helix content is 6.71 % due to apigenin-induced conformational perturbations.
  • The energy transfer efficiency decreases from 27.42 % to 11.46 % upon coexistence of benazepril and apigenin with BSA.
  • The binding distance increases from 2.82 nm to 3.37 nm upon coexistence of benazepril and apigenin with BSA.
  • The fluorescence spectra blueshift by 3.0 nm upon apigenin-induced disruption of BSA's secondary structure.

Sources:

  • Spectrochimica Acta Part A (2025; 347: 127050)
  • Pergamon-elsevier Science Ltd (The Boulevard, Langford Lane, Kidlington, Oxford OX5 1GB, England)
  • Bohai University (College of Chemistry and Chemical Engineering, Jinzhou 121013, People's Republic of China)
  • Xinying Yuan (College of Chemistry and Chemical Engineering, Bohai University, Jinzhou 121013, People's Republic of China)
  • Xue Li, Shijun Yu, and Jiali Gu (Bohai University, Jinzhou, People's Republic of China)

Read more