<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Gutierrez DA</submitter><funding>NCRR NIH HHS</funding><funding>NIH/ORIP</funding><funding>NCRR/Viper</funding><funding>NIH</funding><funding>NIH HHS</funding><funding>NSF-REU</funding><funding>NIGMS NIH HHS</funding><pagination>1-7</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5175404</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>124</volume><pubmed_abstract>We have demonstrated in previous studies that a single amino acid change can alter the activity of the recombinant disintegrin r-Moj. In this study, four r-Moj recombinants containing single mutations (r-Moj-WL, r-Moj-WM, r-Moj-WP, r-Moj-MN) and two containing double mutations (r-Moj-MP and r-Moj-NM) at the binding loop were produced, purified, and tested. All r-Moj-W_, r-Moj-M_, and r-Moj-NM mutant peptides inhibited platelet aggregation at higher potency than r-Moj-D_ mutants. Five of the seven r-Moj peptides inhibited angiogenesis at different levels. Two of the mutant peptides with a methionine at the second position carboxyl of the RGD (r-Moj-WM and r-Moj-NM) were the strongest angiogenesis inhibitors, with r-Moj-WM being the most potent. Recombinant r-Moj-MP and r-Moj-WN failed to in</pubmed_abstract><journal>Toxicon : official journal of the International Society on Toxinology</journal><pubmed_title>Functional analysis of four single (RGDWL, RGDWM, RGDWP, RGDMN) and two double (RGDNM, RGDMP) mutants: The importance of methionine (M) in the functional potency of recombinant mojastin (r-Moj).</pubmed_title><pmcid>PMC5175404</pmcid><funding_grant_id>5T34GM008253-27</funding_grant_id><funding_grant_id>R25GM071381</funding_grant_id><funding_grant_id>5R25GM71381</funding_grant_id><funding_grant_id>T34 GM008253</funding_grant_id><funding_grant_id>5P40OD010960</funding_grant_id><funding_grant_id>2P40RR018300</funding_grant_id><funding_grant_id>DBI 1004350</funding_grant_id><funding_grant_id>P40 OD010960</funding_grant_id><funding_grant_id>R25 GM071381</funding_grant_id><funding_grant_id>P40 RR018300</funding_grant_id><pubmed_authors>Sanchez EE</pubmed_authors><pubmed_authors>Aranda AS</pubmed_authors><pubmed_authors>Soto JG</pubmed_authors><pubmed_authors>Lucena SE</pubmed_authors><pubmed_authors>Koshlaychuk MA</pubmed_authors><pubmed_authors>Carrillo DA</pubmed_authors><pubmed_authors>Gutierrez DA</pubmed_authors></additional><is_claimable>false</is_claimable><name>Functional analysis of four single (RGDWL, RGDWM, RGDWP, RGDMN) and two double (RGDNM, RGDMP) mutants: The importance of methionine (M) in the functional potency of recombinant mojastin (r-Moj).</name><description>We have demonstrated in previous studies that a single amino acid change can alter the activity of the recombinant disintegrin r-Moj. In this study, four r-Moj recombinants containing single mutations (r-Moj-WL, r-Moj-WM, r-Moj-WP, r-Moj-MN) and two containing double mutations (r-Moj-MP and r-Moj-NM) at the binding loop were produced, purified, and tested. All r-Moj-W_, r-Moj-M_, and r-Moj-NM mutant peptides inhibited platelet aggregation at higher potency than r-Moj-D_ mutants. Five of the seven r-Moj peptides inhibited angiogenesis at different levels. Two of the mutant peptides with a methionine at the second position carboxyl of the RGD (r-Moj-WM and r-Moj-NM) were the strongest angiogenesis inhibitors, with r-Moj-WM being the most potent. Recombinant r-Moj-MP and r-Moj-WN failed to in</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Dec</publication><modification>2025-04-18T17:44:58.747Z</modification><creation>2019-03-27T02:32:12Z</creation></dates><accession>S-EPMC5175404</accession><cross_references><pubmed>27816535</pubmed><doi>10.1016/j.toxicon.2016.11.002</doi></cross_references></HashMap>