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Mechanism of angiotensin converting enzyme (ACE) inhibition by Syzygium polyanthum wight (WALP.) leaves

Syzygium polyanthum is an ethnomedicinal plant used for the treatment of hypertension. This study investigates its antihypertensive property using angiotensin-converting enzyme (ACE) enzyme inhibition assay. This study aims to determine the ACE inhibitory activity of S. polyanthum leaves aqueous ext...

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Main Authors: Tuan Anuar, Tuan Ashraf Faiz, Ismail, Azlini, Mohamed Suffian, Izzat Fahimuddin, Abdul Hamid, Azzmer Azzar, Omar, Muhammad Nor, Mustafa Al-Ahmad, Basma Ezzat, Wan Ahmad, Wan Amir Nizam
Format: Conference or Workshop Item
Language:English
English
Published: 2021
Subjects:
QD Chemistry
RM Therapeutics. Pharmacology
RM300 Drugs and their action
Online Access:http://irep.iium.edu.my/95587/1/IRD%20book%202021_Final.pdf
http://irep.iium.edu.my/95587/7/Slide%20IRD2021%20%28Faiz%29.pdf
http://irep.iium.edu.my/95587/
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spelling my.iium.irep.955872021-12-31T00:31:00Z http://irep.iium.edu.my/95587/ Mechanism of angiotensin converting enzyme (ACE) inhibition by Syzygium polyanthum wight (WALP.) leaves Tuan Anuar, Tuan Ashraf Faiz Ismail, Azlini Mohamed Suffian, Izzat Fahimuddin Abdul Hamid, Azzmer Azzar Omar, Muhammad Nor Mustafa Al-Ahmad, Basma Ezzat Wan Ahmad, Wan Amir Nizam QD Chemistry RM Therapeutics. Pharmacology RM300 Drugs and their action Syzygium polyanthum is an ethnomedicinal plant used for the treatment of hypertension. This study investigates its antihypertensive property using angiotensin-converting enzyme (ACE) enzyme inhibition assay. This study aims to determine the ACE inhibitory activity of S. polyanthum leaves aqueous extract (ASP), its inhibition specificity and mechanism and the possible bioactive compound. ACE inhibition activity of ASP (1-1000 µg/ml) was tested and compared with standard drug, captopril (2.06 ng/ml). The inhibition mechanism was tested using zinc chloride and bovine serum albumin (BSA). The phytochemical composition in ASP was analyzed using Liquid Chromatography Quadrupole Time-of-Flight Mass Spectrometry. In silico docking analysis was then performed between the major identified compounds in ASP with ACE. ASP at 100 μg/ml exhibited the highest inhibition activity (69.43 ± 0.60%) compared to MSP (41.63 ± 0.15%), EASP (9.62 ± 1.60%) and also HSP (45.40 ± 0.15%). From the dose-response curve for ACE inhibition activity of ASP, the inhibitory concentration of ASP that causes 50% of ACE inhibition activity (IC50) was 41 μg/ml. ACE inhibition activity by ASP was significantly reduced by the presence of BSA, indicative of interaction of ASP with albumin. ACE inhibition activity by ASP was not significantly affected with the presence of zinc chloride, indicating that its inhibitory activity on ACE was non-dependent of zinc at the ACE active site. There were 26 compounds identified in ASP with 1-galloyl-glucose identified as the major compound. Molecular docking analysis showed that 1-galloyl-glucose has lower binding energy (-7.7 kcal/mol) with ACE, as compared to standard drug, captopril (-5.6 kcal/mol); indicative of good interaction between 1-galloyl-glucose and ACE. In conclusion, this study showed that ACE inhibition activity by S. polyanthum leaves possibly occurs via protein precipitation and was non-dependent to the chelation with zinc at ACE active site, with 1-galloyl-glucose suggested as the potential bioactive compound. 2021-11-24 Conference or Workshop Item NonPeerReviewed application/pdf en http://irep.iium.edu.my/95587/1/IRD%20book%202021_Final.pdf application/pdf en http://irep.iium.edu.my/95587/7/Slide%20IRD2021%20%28Faiz%29.pdf Tuan Anuar, Tuan Ashraf Faiz and Ismail, Azlini and Mohamed Suffian, Izzat Fahimuddin and Abdul Hamid, Azzmer Azzar and Omar, Muhammad Nor and Mustafa Al-Ahmad, Basma Ezzat and Wan Ahmad, Wan Amir Nizam (2021) Mechanism of angiotensin converting enzyme (ACE) inhibition by Syzygium polyanthum wight (WALP.) leaves. In: IIUM Research Day 2021: An International Online Event for Life Sciences, 24th November 2021, Kuantan, Pahang. (Unpublished)
institution Universiti Islam Antarabangsa Malaysia
building IIUM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider International Islamic University Malaysia
content_source IIUM Repository (IREP)
url_provider http://irep.iium.edu.my/
language English
English
topic QD Chemistry
RM Therapeutics. Pharmacology
RM300 Drugs and their action
spellingShingle QD Chemistry
RM Therapeutics. Pharmacology
RM300 Drugs and their action
Tuan Anuar, Tuan Ashraf Faiz
Ismail, Azlini
Mohamed Suffian, Izzat Fahimuddin
Abdul Hamid, Azzmer Azzar
Omar, Muhammad Nor
Mustafa Al-Ahmad, Basma Ezzat
Wan Ahmad, Wan Amir Nizam
Mechanism of angiotensin converting enzyme (ACE) inhibition by Syzygium polyanthum wight (WALP.) leaves
description Syzygium polyanthum is an ethnomedicinal plant used for the treatment of hypertension. This study investigates its antihypertensive property using angiotensin-converting enzyme (ACE) enzyme inhibition assay. This study aims to determine the ACE inhibitory activity of S. polyanthum leaves aqueous extract (ASP), its inhibition specificity and mechanism and the possible bioactive compound. ACE inhibition activity of ASP (1-1000 µg/ml) was tested and compared with standard drug, captopril (2.06 ng/ml). The inhibition mechanism was tested using zinc chloride and bovine serum albumin (BSA). The phytochemical composition in ASP was analyzed using Liquid Chromatography Quadrupole Time-of-Flight Mass Spectrometry. In silico docking analysis was then performed between the major identified compounds in ASP with ACE. ASP at 100 μg/ml exhibited the highest inhibition activity (69.43 ± 0.60%) compared to MSP (41.63 ± 0.15%), EASP (9.62 ± 1.60%) and also HSP (45.40 ± 0.15%). From the dose-response curve for ACE inhibition activity of ASP, the inhibitory concentration of ASP that causes 50% of ACE inhibition activity (IC50) was 41 μg/ml. ACE inhibition activity by ASP was significantly reduced by the presence of BSA, indicative of interaction of ASP with albumin. ACE inhibition activity by ASP was not significantly affected with the presence of zinc chloride, indicating that its inhibitory activity on ACE was non-dependent of zinc at the ACE active site. There were 26 compounds identified in ASP with 1-galloyl-glucose identified as the major compound. Molecular docking analysis showed that 1-galloyl-glucose has lower binding energy (-7.7 kcal/mol) with ACE, as compared to standard drug, captopril (-5.6 kcal/mol); indicative of good interaction between 1-galloyl-glucose and ACE. In conclusion, this study showed that ACE inhibition activity by S. polyanthum leaves possibly occurs via protein precipitation and was non-dependent to the chelation with zinc at ACE active site, with 1-galloyl-glucose suggested as the potential bioactive compound.
format Conference or Workshop Item
author Tuan Anuar, Tuan Ashraf Faiz
Ismail, Azlini
Mohamed Suffian, Izzat Fahimuddin
Abdul Hamid, Azzmer Azzar
Omar, Muhammad Nor
Mustafa Al-Ahmad, Basma Ezzat
Wan Ahmad, Wan Amir Nizam
author_facet Tuan Anuar, Tuan Ashraf Faiz
Ismail, Azlini
Mohamed Suffian, Izzat Fahimuddin
Abdul Hamid, Azzmer Azzar
Omar, Muhammad Nor
Mustafa Al-Ahmad, Basma Ezzat
Wan Ahmad, Wan Amir Nizam
author_sort Tuan Anuar, Tuan Ashraf Faiz
title Mechanism of angiotensin converting enzyme (ACE) inhibition by Syzygium polyanthum wight (WALP.) leaves
title_short Mechanism of angiotensin converting enzyme (ACE) inhibition by Syzygium polyanthum wight (WALP.) leaves
title_full Mechanism of angiotensin converting enzyme (ACE) inhibition by Syzygium polyanthum wight (WALP.) leaves
title_fullStr Mechanism of angiotensin converting enzyme (ACE) inhibition by Syzygium polyanthum wight (WALP.) leaves
title_full_unstemmed Mechanism of angiotensin converting enzyme (ACE) inhibition by Syzygium polyanthum wight (WALP.) leaves
title_sort mechanism of angiotensin converting enzyme (ace) inhibition by syzygium polyanthum wight (walp.) leaves
publishDate 2021
url http://irep.iium.edu.my/95587/1/IRD%20book%202021_Final.pdf
http://irep.iium.edu.my/95587/7/Slide%20IRD2021%20%28Faiz%29.pdf
http://irep.iium.edu.my/95587/
_version_ 1720979925010219008
score 13.211869

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