<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Wynn JE</submitter><funding>National Institute of General Medical Sciences</funding><funding>NIGMS NIH HHS</funding><pagination>820-823</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5554892</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>8(8)</volume><pubmed_abstract>The emergence of microbial resistance presents a challenge in the development of next generation therapeutics. Herein, we report the discovery of branched peptides decorated with acridine and boronic acid moieties with potent antimicrobial activity. The results revealed minimal inhibitory concentrations (MICs) as low as 1 μg/mL against &lt;i>Staphylococcus aureus&lt;/i>, &lt;i>Candida albicans&lt;/i>, and &lt;i>Escherichia coli&lt;/i>. These peptides were nonhemolytic, and significantly inhibited growth of &lt;i>C. albicans&lt;/i> in suspension and biofilm formation. Structure-activity relationship studies suggest the acridine functional group as a driving force for the potent inhibition observed against bacteria.</pubmed_abstract><journal>ACS medicinal chemistry letters</journal><pubmed_title>Branched Peptides: Acridine and Boronic Acid Derivatives as Antimicrobial Agents.</pubmed_title><pmcid>PMC5554892</pmcid><funding_grant_id>R01 GM093834</funding_grant_id><pubmed_authors>Wynn JE</pubmed_authors><pubmed_authors>Zhang W</pubmed_authors><pubmed_authors>Falkinham JO</pubmed_authors><pubmed_authors>Santos WL</pubmed_authors></additional><is_claimable>false</is_claimable><name>Branched Peptides: Acridine and Boronic Acid Derivatives as Antimicrobial Agents.</name><description>The emergence of microbial resistance presents a challenge in the development of next generation therapeutics. Herein, we report the discovery of branched peptides decorated with acridine and boronic acid moieties with potent antimicrobial activity. The results revealed minimal inhibitory concentrations (MICs) as low as 1 μg/mL against &lt;i>Staphylococcus aureus&lt;/i>, &lt;i>Candida albicans&lt;/i>, and &lt;i>Escherichia coli&lt;/i>. These peptides were nonhemolytic, and significantly inhibited growth of &lt;i>C. albicans&lt;/i> in suspension and biofilm formation. Structure-activity relationship studies suggest the acridine functional group as a driving force for the potent inhibition observed against bacteria.</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Aug</publication><modification>2024-11-12T17:59:41.875Z</modification><creation>2019-03-26T23:50:06Z</creation></dates><accession>S-EPMC5554892</accession><cross_references><pubmed>28835795</pubmed><doi>10.1021/acsmedchemlett.7b00119</doi></cross_references></HashMap>