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<p>Thrombin is a core enzyme in the coagulation system, and inhibiting its activity can improve the hypercoagulable state of blood, playing a crucial role in the prevention and treatment of thrombotic diseases. The main objectives of this study were to isolate and characterize a thrombin-inhibitory peptide from Diospyros lotus(<i>D. lotus</i>) pomace and to evaluate its synergistic effect with gallic acid (GA) through in vitro assays. After enzymatic hydrolysis of proteins from <i>D. lotus</i> pomace followed by ultrafiltration purification, a total of 266 peptides were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS), from which virtual screening identified the most bioactive peptide, Pro-Pro-His-Gly (PPHG). Although PPHG exhibited a relatively high IC₅₀ of 30.69 ± 0.54&#xa0;mg/mL against thrombin compared to conventional bioactives, its combination with GA (4&#xa0;mg/mL) at 10&#xa0;mg/mL produced a marked synergistic effect, enabling a reduction in the effective dose of PPHG. Fourier-transform infrared spectroscopy (FTIR) revealed the formation of hydrogen bonds between PPHG and GA, Circular dichroism (CD) spectroscopy demonstrated that PPHG and GA affected thrombin activity by altering its secondary structure, with a stronger effect when combined. These results indicate that PPHG and GA have a synergistic anticoagulant effect, holding promise for application in the treatment of thrombotic diseases and the development of functional foods.</p> Graphical Abstract <p></p>

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Synergistic thrombin inhibition by Diospyros lotus pomace peptides and gallic acid: an in vitro assessment of effects and mechanisms

  • 期刊论文

  • 发表日期：

    2025年12月2日

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  • Zhen-Wei Shi,
  • Hong-Hong Cai,
  • Hai-Bin Ren,
  • Xiao-Ning Shang,
  • Si-Yang An,
  • Di-Feng Ren

摘要

Thrombin is a core enzyme in the coagulation system, and inhibiting its activity can improve the hypercoagulable state of blood, playing a crucial role in the prevention and treatment of thrombotic diseases. The main objectives of this study were to isolate and characterize a thrombin-inhibitory peptide from Diospyros lotus(D. lotus) pomace and to evaluate its synergistic effect with gallic acid (GA) through in vitro assays. After enzymatic hydrolysis of proteins from D. lotus pomace followed by ultrafiltration purification, a total of 266 peptides were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS), from which virtual screening identified the most bioactive peptide, Pro-Pro-His-Gly (PPHG). Although PPHG exhibited a relatively high IC₅₀ of 30.69 ± 0.54 mg/mL against thrombin compared to conventional bioactives, its combination with GA (4 mg/mL) at 10 mg/mL produced a marked synergistic effect, enabling a reduction in the effective dose of PPHG. Fourier-transform infrared spectroscopy (FTIR) revealed the formation of hydrogen bonds between PPHG and GA, Circular dichroism (CD) spectroscopy demonstrated that PPHG and GA affected thrombin activity by altering its secondary structure, with a stronger effect when combined. These results indicate that PPHG and GA have a synergistic anticoagulant effect, holding promise for application in the treatment of thrombotic diseases and the development of functional foods.

Graphical Abstract