Marine Drugs (Sep 2023)

Affinity Purification and Molecular Characterization of Angiotensin-Converting Enzyme (ACE)-Inhibitory Peptides from <i>Takifugu flavidus</i>

  • Yongchang Su,
  • Shicheng Chen,
  • Shuji Liu,
  • Yin Wang,
  • Xiaoting Chen,
  • Min Xu,
  • Shuilin Cai,
  • Nan Pan,
  • Kun Qiao,
  • Bei Chen,
  • Suping Yang,
  • Zhiyu Liu

DOI
https://doi.org/10.3390/md21100522
Journal volume & issue
Vol. 21, no. 10
p. 522

Abstract

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An affinity chromatography filler of CNBr-activated Sepharose 4B-immobilized ACE was used to purify ACE-inhibitory peptides from Takifugu flavidus protein hydrolysate (50 = 93.5 µmol·L−1) was selected. Molecular docking revealed that TLRFALHGME may interact with the active site of ACE through H-bond, hydrophobic, and electrostatic interactions. The total binding energy (ΔGbinding) of TLRFALHGME was estimated to be −82.7382 kJ·mol−1 by MD simulations, indicating the favorable binding of peptides with ACE. Furthermore, the binding affinity of TLRFALHGME to ACE was determined by surface plasmon resonance (SPR) with a Kd of 80.9 µmol, indicating that there was a direct molecular interaction between them. TLRFALHGME has great potential for the treatment of hypertension.

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