A Novel Angiotensin-I-Converting Enzyme (ACE) Inhibitory Peptide from <i>Takifugu flavidus</i>
Yongchang Su,
Shicheng Chen,
Shuilin Cai,
Shuji Liu,
Nan Pan,
Jie Su,
Kun Qiao,
Min Xu,
Bei Chen,
Suping Yang,
Zhiyu Liu
Affiliations
Yongchang Su
College of Chemical Engineering, Huaqiao University, Xiamen 361021, China
Shicheng Chen
Department of Clinical and Diagnostic Sciences, School of Health Sciences, Oakland University, 433 Meadowbrook Road, Rochester, MI 48309, USA
Shuilin Cai
College of Chemical Engineering, Huaqiao University, Xiamen 361021, China
Shuji Liu
Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China
Nan Pan
Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China
Jie Su
Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China
Kun Qiao
Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China
Min Xu
Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China
Bei Chen
Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China
Suping Yang
College of Chemical Engineering, Huaqiao University, Xiamen 361021, China
Zhiyu Liu
Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, Fisheries Research Institute of Fujian, Xiamen 361013, China
Alcalase, neutral protease, and pepsin were used to hydrolyze the skin of Takifugu flavidus. The T. flavidus hydrolysates (TFHs) with the maximum degree of hydrolysis (DH) and angiotensin-I-converting enzyme (ACE)-inhibitory activity were selected and then ultra-filtered to obtain fractions with components of different molecular weights (MWs) (50 kDa). The components with MWs 50) of 0.58 mg/mL. Purification and identification using semi-preparative liquid chromatography, Sephadex G-15 gel chromatography, RP-HPLC, and LC–MS/MS yielded one new potential ACE-inhibitory peptide, PPLLFAAL (non-competitive suppression mode; IC50 of 28 μmmol·L−1). Molecular docking and molecular dynamics simulations indicated that the peptides should bind well to ACE and interact with amino acid residues and the zinc ion at the ACE active site. Furthermore, a short-term assay of antihypertensive activity in spontaneously hypertensive rats (SHRs) revealed that PPLLFAAL could significantly decrease the systolic blood pressure (SBP) and diastolic blood pressure (DBP) of SHRs after intravenous administration. These results suggested that PPLLFAAL may have potential applications in functional foods or pharmaceuticals as an antihypertensive agent.
