Abstract
Abstract Background Many short peptides have proved to exhibit potential anti-hypertensive activity through the inhibition of the Angiotensin I-converting enzyme (ACE) activity and the regulation of blood pressure. However, the traditional experimental screening method for ACE inhibitory peptides is time consuming and costly, accompanied with the limitations as incomplete hydrolysis and peptides loss during purification process. Virtual methods with the aid of computer can break such bottle-neck of experimental work. In this study, an attempt was made to establish a library of di- and tri-peptides derived from proteins of Phascolosoma esculenta, a kind of seafood, through BIOPEP (http://www.uwm.edu.pl/biochemia/index.php/pl/biopep), and to screen highly active ACE inhibitory peptides by molecular docking with the help of LibDock module of Discovery Studio 3.5 software. Results Two hundred and eighty four (284) di- and tri-peptides, derived from P. esculenta proteins after a virtual hydrolysis with pepsin, trypsin and a mixture of pepsin and trypsin, were predicted to possess ACE inhibitory activity, among which there are 99 ACE inhibitory peptides with estimated IC50 less than 50 μM. Nine peptides were synthesized for the comparison between the estimated and the experimentally determined IC50. The results indicated that errors between the estimated and measured log(1/IC50) are all less than 1.0 unit. Conclusions Virtual method for peptide library construction and ACE inhibitory peptides screening efficiently demonstrated that P. esculenta proteins are prospect resource for food-origin ACE inhibitory peptide.
Highlights
Many short peptides have proved to exhibit potential anti-hypertensive activity through the inhibition of the Angiotensin I-converting enzyme (ACE) activity and the regulation of blood pressure
Pool of di- and tri-peptides derived from P. esculenta proteins Pepsin, trypsin, and the mixture of pepsin and trypsin were used to virtually hydrolyze the 22 proteins from P. esculenta, with the help of BIOPEP
These 284 peptides were used as the ligands for docking experiment with ACE
Summary
Many short peptides have proved to exhibit potential anti-hypertensive activity through the inhibition of the Angiotensin I-converting enzyme (ACE) activity and the regulation of blood pressure. The traditional experimental screening method for ACE inhibitory peptides is time consuming and costly, accompanied with the limitations as incomplete hydrolysis and peptides loss during purification process. An attempt was made to establish a library of di- and tri-peptides derived from proteins of Phascolosoma esculenta, a kind of seafood, through BIOPEP (http://www.uwm.edu.pl/biochemia/index.php/pl/biopep), and to screen highly active ACE inhibitory peptides by molecular docking with the help of LibDock module of Discovery Studio 3.5 software. The cause of hypertension currently cannot be well determined, it is understood that the reninangiotensin system regulates an organism's water, electrolytes, and blood, and the angiotensin I-converting enzyme (ACE) (peptidyldipeptide hydrolase, EC 3.4.15.1) plays an. Nutritionists claim that peptides found in food are safer than ‘traditional’ drugs, and they are promising synthetic drug substitutes [26]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
