<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ding Z</submitter><funding>National Key Research and Development Program</funding><pagination>5421</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9457961</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>27(17)</volume><pubmed_abstract>The renin-angiotensin system (RAS) is the primary pathway for regulating blood pressure in the body, and angiotensin-converting enzymes (ACEs) play a crucial role in it. &lt;i>Hirudo nipponia&lt;/i> is an invertebrate that contains a variety of active peptides; however, there are no studies on the ACE inhibitory activity of hirudo. In the present study, our aim was to identify the active peptides in hirudo based on active peptide database analysis, unexpectedly filling the gap in hirudo ACE inhibitory activity research. Prep-HPLC was used to separate the part below 3 kD from hirudo. The peptide composition of the isolates was obtained based on Orbitrap LC-MS. The activity of each group of peptides was predicted by the database and the activity was determined by bioassay. Peptides with validation</pubmed_abstract><journal>Molecules (Basel, Switzerland)</journal><pubmed_title>Research on ACEI of Low-Molecular-Weight Peptides from &lt;i>Hirudo nipponia&lt;/i> Whitman.</pubmed_title><pmcid>PMC9457961</pmcid><funding_grant_id>2017YFC1701003</funding_grant_id><funding_grant_id>SQ2017YFC170086-3</funding_grant_id><pubmed_authors>Chen K</pubmed_authors><pubmed_authors>Chen Y</pubmed_authors><pubmed_authors>Ding Z</pubmed_authors></additional><is_claimable>false</is_claimable><name>Research on ACEI of Low-Molecular-Weight Peptides from &lt;i>Hirudo nipponia&lt;/i> Whitman.</name><description>The renin-angiotensin system (RAS) is the primary pathway for regulating blood pressure in the body, and angiotensin-converting enzymes (ACEs) play a crucial role in it. &lt;i>Hirudo nipponia&lt;/i> is an invertebrate that contains a variety of active peptides; however, there are no studies on the ACE inhibitory activity of hirudo. In the present study, our aim was to identify the active peptides in hirudo based on active peptide database analysis, unexpectedly filling the gap in hirudo ACE inhibitory activity research. Prep-HPLC was used to separate the part below 3 kD from hirudo. The peptide composition of the isolates was obtained based on Orbitrap LC-MS. The activity of each group of peptides was predicted by the database and the activity was determined by bioassay. Peptides with validation</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Aug</publication><modification>2026-05-10T03:19:54.89Z</modification><creation>2024-11-15T17:34:56.263Z</creation></dates><accession>S-EPMC9457961</accession><cross_references><pubmed>36080189</pubmed><doi>10.3390/molecules27175421</doi></cross_references></HashMap>