Ala-Val-Phe and Val-Phe: ACE inhibitory peptides derived from insect protein with antihypertensive activity in spontaneously hypertensive rats

Peptides ◽  
2010 ◽  
Vol 31 (3) ◽  
pp. 482-488 ◽  
Author(s):  
Lieselot Vercruysse ◽  
John Van Camp ◽  
Nicole Morel ◽  
Pierre Rougé ◽  
Griet Herregods ◽  
...  
Marine Drugs ◽  
2018 ◽  
Vol 16 (9) ◽  
pp. 299 ◽  
Author(s):  
Zhenzhen Deng ◽  
Yingjuan Liu ◽  
Jing Wang ◽  
Suhuang Wu ◽  
Lihua Geng ◽  
...  

A variety of biologically active products have been isolated from Gracilariopsis lemaneiformis. In the present study, two novel angiotensin-converting enzyme (ACE) inhibitory peptides, FQIN [M(O)] CILR, and TGAPCR, were screened and identified from G. lemaneiformis protein hydrolysates by LC-MS/MS. The IC50 values of FQIN [M(O)] CILR and TGAPCR were 9.64 ± 0.36 μM and 23.94 ± 0.82 μM, respectively. In the stability study, both peptides showed stabilities of pH, temperature, simulated gastrointestinal digestion, and ACE hydrolysis. The Lineweaver–Burk plot showed that the two peptides were noncompetitive inhibitors of ACE. Molecular docking simulated the intermolecular interactions of two peptides and ACE, and the two peptides formed hydrogen bonds with the active pockets of ACE. However, FQIN [M(O)] CILR was more closely linked to the active pockets of ACE, thereby exerting better ACE inhibition. Spontaneously hypertensive rats (SHRs) were studied with an oral dose of 10 mg/kg body weight. Both peptides reduced systolic blood pressure (SBP) and diastolic blood pressure (DBP) in SHRs, of which FQIN [M(O)] CILR was able to reduce the systolic blood pressure by 34 mmHg (SBP) (p < 0.05). Therefore, FQIN [M(O)] CILR was an excellent ACE inhibitory peptide.


2015 ◽  
Vol 13 ◽  
pp. 50-60 ◽  
Author(s):  
Kaustav Majumder ◽  
Subhadeep Chakrabarti ◽  
Jude S. Morton ◽  
Sareh Panahi ◽  
Susan Kaufman ◽  
...  

Nutrients ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 271 ◽  
Author(s):  
Juan María Alcaide-Hidalgo ◽  
Miguel Romero ◽  
Juan Duarte ◽  
Eduardo López-Huertas

The low molecular weight peptide composition of virgin olive oil (VOO) is mostly unknown. We hypothesised that unfiltered VOO could possess low molecular weight peptides with antihypertensive activity. We produced unfiltered VOO and obtained a water-soluble peptide extract from it. The peptides were separated by size-exclusion using fast protein liquid chromatography, and the low molecular weight fraction was analysed by nanoscale liquid chromatography-Orbitrap coupled with tandem mass spectrometry and de novo sequencing. We selected 23 peptide sequences containing between 6 and 9 amino acids and molecular masses ranging 698–1017 Da. Those peptides were chemically synthesised and their angiotensin-converting enzyme (ACE) inhibitory activity was studied in vitro. Seven peptides showed a strong activity, with half maximal inhibitory concentration (IC50) <10 µm. The antihypertensive effects of the four most active synthesised ACE inhibitor peptides were studied in spontaneously hypertensive rats (SHR). Acute oral administration of synthetic peptides RDGGYCC and CCGNAVPQ showed antihypertensive activity in SHR. We conclude that unfiltered VOO naturally contains low molecular weight peptides with specific ACE inhibitory activity and antihypertensive effects in SHR.


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