In vitro antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins

© 2020 Institute of Food Science and Technology New bioactive peptides with antihypertensive property from red blood corpuscle (RBC) and plasma (PL) hydrolysate fractions of porcine blood were identified. Three peptides with the highest Angiotensin-converting enzyme (ACE) inhibitory activity from RB...

Full description

Saved in:
Bibliographic Details
Main Authors: Panida Aiemratchanee, Kulachatr Panyawechamontri, Phutthaphorn Phaophu, Onrapak Reamtong, Watanalai Panbangred
Other Authors: Mahidol University
Format: Article
Published: 2020
Subjects:
Online Access:https://repository.li.mahidol.ac.th/handle/123456789/60363
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Mahidol University
id th-mahidol.60363
record_format dspace
spelling th-mahidol.603632020-12-28T12:18:33Z In vitro antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins Panida Aiemratchanee Kulachatr Panyawechamontri Phutthaphorn Phaophu Onrapak Reamtong Watanalai Panbangred Mahidol University Betagro Science Center Co. Agricultural and Biological Sciences Engineering © 2020 Institute of Food Science and Technology New bioactive peptides with antihypertensive property from red blood corpuscle (RBC) and plasma (PL) hydrolysate fractions of porcine blood were identified. Three peptides with the highest Angiotensin-converting enzyme (ACE) inhibitory activity from RBC, including RBC7 (TPYPCV), RBC15 (VVYPWR) and RBC9 (FLCT), showed IC50 values of 2.58 ± 0.87, 5.22 ± 2.56 and 6.53 ± 0.34 µm, respectively. By comparison, PL1 (YTFPFH), PL2 (WGHGNPHV) and PL7 (VPLW) from PL displayed higher IC50 values at 24.12 ± 2.44, 15.33 ± 0.44 and 32.80 ± 38.96 µm, respectively. Molecular docking was employed to simulate the interactions of RBC7 and RBC15 with the catalytic site of the ACE receptor. RBC7 and RBC15 interacted with residues in the ACE receptor that normally coordinated with Zn(II), and RBC7 also interacted extensively with residues within S1, S2 and S’1 active sites. Taken together, these results illustrate that porcine blood is an excellent source of antihypertensive peptides and could be of great benefits to people with high blood pressure. 2020-12-28T03:54:32Z 2020-12-28T03:54:32Z 2020-01-01 Article International Journal of Food Science and Technology. (2020) 10.1111/ijfs.14853 13652621 09505423 2-s2.0-85096689850 https://repository.li.mahidol.ac.th/handle/123456789/60363 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85096689850&origin=inward
institution Mahidol University
building Mahidol University Library
continent Asia
country Thailand
Thailand
content_provider Mahidol University Library
collection Mahidol University Institutional Repository
topic Agricultural and Biological Sciences
Engineering
spellingShingle Agricultural and Biological Sciences
Engineering
Panida Aiemratchanee
Kulachatr Panyawechamontri
Phutthaphorn Phaophu
Onrapak Reamtong
Watanalai Panbangred
In vitro antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins
description © 2020 Institute of Food Science and Technology New bioactive peptides with antihypertensive property from red blood corpuscle (RBC) and plasma (PL) hydrolysate fractions of porcine blood were identified. Three peptides with the highest Angiotensin-converting enzyme (ACE) inhibitory activity from RBC, including RBC7 (TPYPCV), RBC15 (VVYPWR) and RBC9 (FLCT), showed IC50 values of 2.58 ± 0.87, 5.22 ± 2.56 and 6.53 ± 0.34 µm, respectively. By comparison, PL1 (YTFPFH), PL2 (WGHGNPHV) and PL7 (VPLW) from PL displayed higher IC50 values at 24.12 ± 2.44, 15.33 ± 0.44 and 32.80 ± 38.96 µm, respectively. Molecular docking was employed to simulate the interactions of RBC7 and RBC15 with the catalytic site of the ACE receptor. RBC7 and RBC15 interacted with residues in the ACE receptor that normally coordinated with Zn(II), and RBC7 also interacted extensively with residues within S1, S2 and S’1 active sites. Taken together, these results illustrate that porcine blood is an excellent source of antihypertensive peptides and could be of great benefits to people with high blood pressure.
author2 Mahidol University
author_facet Mahidol University
Panida Aiemratchanee
Kulachatr Panyawechamontri
Phutthaphorn Phaophu
Onrapak Reamtong
Watanalai Panbangred
format Article
author Panida Aiemratchanee
Kulachatr Panyawechamontri
Phutthaphorn Phaophu
Onrapak Reamtong
Watanalai Panbangred
author_sort Panida Aiemratchanee
title In vitro antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins
title_short In vitro antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins
title_full In vitro antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins
title_fullStr In vitro antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins
title_full_unstemmed In vitro antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins
title_sort in vitro antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins
publishDate 2020
url https://repository.li.mahidol.ac.th/handle/123456789/60363
_version_ 1763493121315831808