{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gutierrez DA"],"funding":["NCRR NIH HHS","NIH/ORIP","NCRR/Viper","NIH","NIH HHS","NSF-REU","NIGMS NIH HHS"],"pagination":["1-7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5175404"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["124"],"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"],"journal":["Toxicon : official journal of the International Society on Toxinology"],"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)."],"pmcid":["PMC5175404"],"funding_grant_id":["5T34GM008253-27","R25GM071381","5R25GM71381","T34 GM008253","5P40OD010960","2P40RR018300","DBI 1004350","P40 OD010960","R25 GM071381","P40 RR018300"],"pubmed_authors":["Sanchez EE","Aranda AS","Soto JG","Lucena SE","Koshlaychuk MA","Carrillo DA","Gutierrez DA"],"additional_accession":[]},"is_claimable":false,"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).","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","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Dec","modification":"2025-04-18T17:44:58.747Z","creation":"2019-03-27T02:32:12Z"},"accession":"S-EPMC5175404","cross_references":{"pubmed":["27816535"],"doi":["10.1016/j.toxicon.2016.11.002"]}}