<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Renaudet O</dc:creator>
  <dc:creator>Reymond JL</dc:creator>
  <dc:date>2004</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">[structure: see text] Hydroxyaromatic aldehydes and ketones were used as building blocks to prepare ether oligomers. An iterative two-step protocol involving Mitsunobu coupling and carbonyl reduction provided a protecting-group-free route with high yields. Activity screening of an 84-member library against proteases led to the discovery of micromolar inhibitors for trypsin, chymotrypsin, and subtilisin.</dc:description>
  <dc:identifier>https://sonar.ch/global/documents/131309</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1021/ol036300d</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/14748602</dc:relation>
  <dc:source>Organic letters. - 2004</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Aldehydes</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Chymotrypsin</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Ethers</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Ketones</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Models, Molecular</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Molecular Conformation</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Oximes</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Protease Inhibitors</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Subtilisin</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Trypsin</dc:subject>
  <dc:title xmlns:ns11="xml" ns11:lang="en">Synthesis of ether oligomers.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
