<HashMap><database>biostudies-literature</database><scores/><additional><submitter>MacPherson DS</submitter><funding>NIBIB NIH HHS</funding><funding>Air Force Research Laboratory</funding><funding>NCI NIH HHS</funding><funding>National Science Foundation</funding><pagination>579-587</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9153392</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>8(2)</volume><pubmed_abstract>Matrix metalloproteinase (MMP) enzymes are over-expressed by some metastatic cancers, in which they are responsible for the degradation and remodeling of the extracellular matrix. In recent years, MMPs have emerged as promising targets for enzyme-responsive diagnostic probes because oligopeptides can be designed to be selectively hydrolyzed by exposure to these enzymes. With the ultimate goal of developing radio-iodinated peptides as supramolecular building blocks for MMP-sensitive tools for nuclear imaging and therapy, we designed three MMP-9-responsive peptides containing either tyrosine or iodotyrosine to assess the impact of iodotyrosine introduction to the peptide structure and cleavage kinetics. We found that the peptides containing iodotyrosine underwent more rapid and more complete</pubmed_abstract><journal>ACS biomaterials science &amp; engineering</journal><pubmed_title>The Impact of Tyrosine Iodination on the Aggregation and Cleavage Kinetics of MMP-9-Responsive Peptide Sequences.</pubmed_title><pmcid>PMC9153392</pmcid><funding_grant_id>R01 CA204167</funding_grant_id><funding_grant_id>P30 CA008748</funding_grant_id><funding_grant_id>R21 EB030275</funding_grant_id><funding_grant_id>FA9550-19-1-0111</funding_grant_id><funding_grant_id>HRD-1547830</funding_grant_id><funding_grant_id>R01 CA240963</funding_grant_id><funding_grant_id>U01 CA221046</funding_grant_id><pubmed_authors>McPhee SA</pubmed_authors><pubmed_authors>MacPherson DS</pubmed_authors><pubmed_authors>Ulijn RV</pubmed_authors><pubmed_authors>Zeglis BM</pubmed_authors></additional><is_claimable>false</is_claimable><name>The Impact of Tyrosine Iodination on the Aggregation and Cleavage Kinetics of MMP-9-Responsive Peptide Sequences.</name><description>Matrix metalloproteinase (MMP) enzymes are over-expressed by some metastatic cancers, in which they are responsible for the degradation and remodeling of the extracellular matrix. In recent years, MMPs have emerged as promising targets for enzyme-responsive diagnostic probes because oligopeptides can be designed to be selectively hydrolyzed by exposure to these enzymes. With the ultimate goal of developing radio-iodinated peptides as supramolecular building blocks for MMP-sensitive tools for nuclear imaging and therapy, we designed three MMP-9-responsive peptides containing either tyrosine or iodotyrosine to assess the impact of iodotyrosine introduction to the peptide structure and cleavage kinetics. We found that the peptides containing iodotyrosine underwent more rapid and more complete</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Feb</publication><modification>2025-05-18T12:48:15.794Z</modification><creation>2025-04-04T19:47:38.454Z</creation></dates><accession>S-EPMC9153392</accession><cross_references><pubmed>35050574</pubmed><doi>10.1021/acsbiomaterials.1c01488</doi></cross_references></HashMap>