<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">A Ismail</style></author><author><style face="normal" font="default" size="100%">TAFT Anuar</style></author><author><style face="normal" font="default" size="100%">IFM Suffian</style></author><author><style face="normal" font="default" size="100%">AA Abdul Hamid</style></author><author><style face="normal" font="default" size="100%">MN Omar</style></author><author><style face="normal" font="default" size="100%">BE Mustafa</style></author><author><style face="normal" font="default" size="100%">WAN Wan Ahmad</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Angiotensin Converting Enzyme (ACE) Inhibition Activity by Syzygium polyanthum Wight (Walp.) Leaves: Mechanism and Specificity</style></title><secondary-title><style face="normal" font="default" size="100%">Pharmacognosy Journal</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2022</style></year><pub-dates><date><style  face="normal" font="default" size="100%">February 2022</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">14</style></volume><pages><style face="normal" font="default" size="100%">76-84</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p class=&quot;rtejustify&quot;&gt;&lt;strong&gt;Introduction:&lt;/strong&gt; One of the potential antihypertensive mechanisms include angiotensin converting enzyme (ACE) inhibition. So far, there is no in-depth study on the ACE inhibition activity of &lt;em&gt;S. polyanthum&lt;/em&gt;, an ethnomedicinal plant used in treating hypertension. Thus, we aimed to study the ACE inhibition activity of&lt;em&gt; S. polyanthum&lt;/em&gt; leaves by evaluating its potency, mechanism, and specificity.&lt;strong&gt; Methods: &lt;/strong&gt;&lt;em&gt;S. polyanthum&lt;/em&gt; leaves were macerated in a bath-sonicator with either water, methanol, ethyl acetate, and hexane producing aqueous (ASP), methanolic (MSP), ethyl acetate (EASP) and hexane (HSP) extracts. Each extract (100 μg/mL) were initially screened for ACE inhibition activity and then compared with standard drug, captopril (2.06 ng/mL), then the most active extract was further tested at 1 to 1000μg/ml. Inhibition mechanism was studied using zinc chloride and bovine serum albumin (BSA), while inhibition specificity was determined upon screening for α-chymotrypsin and trypsin inhibition activity. &lt;strong&gt;Results:&lt;/strong&gt; 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 HSP (45.40 ± 0.15 %). ASP showed dose-dependent ACE inhibition activity with IC&lt;sub&gt;50&lt;/sub&gt; of 41 μg/mL. ASP’s ACE inhibition activity was significantly reduced in the presence of BSA, but not upon the presence of zinc chloride. ASP did not significantly inhibit α-chymotrypsin and trypsin. &lt;strong&gt;Conclusion:&lt;/strong&gt; This study showed that the enzyme inhibition activity by&lt;em&gt; S. polyanthum &lt;/em&gt;leaves was specific towards ACE. The ACE inhibition possibly occurs via protein precipitation and was non-dependent to the chelation with zinc at ACE active site.&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;&lt;strong&gt;Key words: &lt;/strong&gt;Antihypertensive, ACE, Angiotensin converting enzyme, Hypertension, Syzygium polyanthum&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><work-type><style face="normal" font="default" size="100%">Original Article</style></work-type><section><style face="normal" font="default" size="100%">76</style></section><auth-address><style face="normal" font="default" size="100%">&lt;p class=&quot;rtejustify&quot;&gt;&lt;strong&gt;A Ismail&lt;sup&gt;1,*&lt;/sup&gt;, TAFT Anuar&lt;sup&gt;2&lt;/sup&gt;, IFM Suffian&lt;sup&gt;3&lt;/sup&gt;, AA Abdul Hamid&lt;sup&gt;4&lt;/sup&gt;, MN Omar&lt;sup&gt;4&lt;/sup&gt;, BE Mustafa&lt;sup&gt;1&lt;/sup&gt;, WAN Wan Ahmad&lt;sup&gt;5&lt;/sup&gt;&lt;/strong&gt;&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;&lt;sup&gt;1&lt;/sup&gt;Department of Fundamental Dental and Medical Sciences, Kulliyah of Dentistry, International Islamic University Malaysia, 25200 Kuantan, Pahang, MALAYSIA.&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;&lt;sup&gt;2&lt;/sup&gt;Department of Chemistry, Kulliyyah of Science, International Islamic University Malaysia, 25200 Kuantan, Pahang, MALAYSIA.&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;&lt;sup&gt;3&lt;/sup&gt;Department of Pharmaceutical Chemistry, Kulliyyah of Pharmacy, International Islamic University Malaysia, 25200 Kuantan, Pahang, MALAYSIA.&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;&lt;sup&gt;4&lt;/sup&gt;Department of Biotechnology, Kulliyyah of Science, International Islamic University Malaysia, 25200 Kuantan, Pahang, MALAYSIA.&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;&lt;sup&gt;5&lt;/sup&gt;Biomedicine Programme, School of Health Sciences, Universiti Sains Malaysia, Health Campus, 16150 Kubang Kerian, Kelantan, MALAYSIA.&lt;/p&gt;
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