Jiali Chen1, Bomi Ryu2, YuanYuan Zhang1, Peng Liang1, Chengyong Li3,4, Chunxia Zhou1, Ping Yang1, Pengzhi Hong1, Zhong-Ji Qian3,4. 1. College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, PR China. 2. Department of Marine Life Sciences, Jeju National University, Jeju, Republic of Korea. 3. School of Chemistry and Environmental Science, Guangdong Ocean University, Zhanjiang, PR China. 4. Shenzhen Institute of Guangdong Ocean University, Shenzhen, PR China.
Abstract
BACKGROUND: In order to utilize tilapia skin gelatin hydrolysate protein, which is normally discarded as industrial waste in the process of fish manufacture, we study the in vivo and in vitro angiotensin-I-converting enzyme (ACE) inhibitory activity of the peptide Leu-Ser-Gly-Tyr-Gly-Pro (LSGYGP). The aim was to provide a pharmacological basis of the development of minimal side effects of ACE inhibitors by comparative analysis with captopril in molecular docking. RESULTS: This peptide from protein-rich wastes showed excellent ACE inhibitory activity (IC50 = 2.577 μmol L-1 ) and exhibited a mixed noncompetitive inhibitory pattern with Lineweaver-Burk plots. Furthermore, LSGYGP and captopril groups both showed significant decreases in blood pressure after 6 h and maintained good digestive stability over 4 h. Molecular bond interactions differentiate competitive captopril upon hydrogen bond interactions and Zn(II) interaction. The C-terminal Pro generates three interactions (hydrogen bonds, hydrophilic interactions and Van der Waals interactions) in the peptide and effectively interacts with the S1 and S2 pockets of ACE. CONCLUSION: LSGYGP, with an IC50 value of 2.577 μmol L-1 , has an antihypertensive effect in spontaneously hypertensive rats. Through comparison with captopril, this study revealed that LSGYGP may be a potential food-derived ACE inhibitory peptide and could act as a functional food ingredient to prevent hypertension.
BACKGROUND: In order to utilize tilapia skin gelatin hydrolysate protein, which is normally discarded as industrial waste in the process of fish manufacture, we study the in vivo and in vitro angiotensin-I-converting enzyme (ACE) inhibitory activity of the peptide Leu-Ser-Gly-Tyr-Gly-Pro (LSGYGP). The aim was to provide a pharmacological basis of the development of minimal side effects of ACE inhibitors by comparative analysis with captopril in molecular docking. RESULTS: This peptide from protein-rich wastes showed excellent ACE inhibitory activity (IC50 = 2.577 μmol L-1 ) and exhibited a mixed noncompetitive inhibitory pattern with Lineweaver-Burk plots. Furthermore, LSGYGP and captopril groups both showed significant decreases in blood pressure after 6 h and maintained good digestive stability over 4 h. Molecular bond interactions differentiate competitive captopril upon hydrogen bond interactions and Zn(II) interaction. The C-terminal Pro generates three interactions (hydrogen bonds, hydrophilic interactions and Van der Waals interactions) in the peptide and effectively interacts with the S1 and S2 pockets of ACE. CONCLUSION: LSGYGP, with an IC50 value of 2.577 μmol L-1 , has an antihypertensive effect in spontaneously hypertensive rats. Through comparison with captopril, this study revealed that LSGYGP may be a potential food-derived ACE inhibitory peptide and could act as a functional food ingredient to prevent hypertension.
Authors: Muhammad Naveed Shahid; Maryam Zawar; Adil Jamal; Bahaeldeen Babiker Mohamed; Sana Khalid; Fayez Saeed Bahwerth Journal: Biomed Res Int Date: 2022-05-23 Impact factor: 3.246
Authors: Gerardo I Arredondo-Mendoza; Zacarías Jiménez-Salas; Francisco Javier Guzmán-de la Garza; Elizabeth Solís-Pérez; Manuel López-Cabanillas-Lomelí; Blanca Edelia González-Martínez; Eduardo Campos-Góngora Journal: Molecules Date: 2020-08-26 Impact factor: 4.411