Activity Analysis and Inhibition Mechanism of Four Novel Angiotensin I-Converting Enzyme Inhibitory Peptides Prepared from Flammulina velutipes by Enzymatic Hydrolysis
2025
Yajie Zhang | Xueqi Zhao | Xia Ma | Jiaqi Li | Xiaoyu Ye | Xuerui Wang | Wenwei Zhang | Jianmin Yun
In order to innovatively develop high-activity ACE inhibitory peptides from edible fungi, the conditions for a double-enzymatic hydrolysis preparation of ACE inhibitory peptides from Flammulina velutipes were optimized by response surface methodology. After purification by macroporous resin, gel chromatography, and RP-HPLC, a crude peptide fraction was obtained: its ACE inhibition rate was 85.73 ±: 0.95% (IC50 = 0.83 ±: 0.09 mg/mL). Based on LC-MS/MS sequencing, the four novel peptides, namely, FAGGP, FDGY, FHPGY, and WADP, were screened by computer analysis and molecular docking technology. The four peptides exhibited a binding energy between &minus:9.4 and &minus:10.3 kcal/mol, and formed hydrogen bonds with Tyr523, Ala354, and Glu384 in the S1 pocket, Tyr520 and His353 in the S2 pocket, and His383 in the HEXXH zinc-coordinating motif of ACE, indicating their good affinity with the ACE active site. The IC50 values of the four ACE inhibitory peptides were 29.17, 91.55, 14.79, and 41.27 &mu:M, respectively, suggesting that these peptides could potentially contribute to the development of new antihypertensive products.
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