1 Ocak 2023 Dergi makalesi Açık Erişim

Yilmaz, Ozgur

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  <identifier identifierType="URL">https://aperta.ulakbim.gov.tr/record/265052</identifier>
  <creators>
    <creator>
      <creatorName>Yilmaz, Ozgur</creatorName>
      <givenName>Ozgur</givenName>
      <familyName>Yilmaz</familyName>
      <affiliation>TUBITAK, Marmara Res Ctr, Mat Technol, TR-41470 Gebze, Kocaeli, Turkiye</affiliation>
    </creator>
  </creators>
  <titles>
    <title>Molecular Modeling, Synthesis And Characterization Of Folr1 Specific Peptides For Tumor Targeting Activity</title>
  </titles>
  <publisher>Aperta</publisher>
  <publicationYear>2023</publicationYear>
  <dates>
    <date dateType="Issued">2023-01-01</date>
  </dates>
  <resourceType resourceTypeGeneral="Text">Journal article</resourceType>
  <alternateIdentifiers>
    <alternateIdentifier alternateIdentifierType="url">https://aperta.ulakbim.gov.tr/record/265052</alternateIdentifier>
  </alternateIdentifiers>
  <relatedIdentifiers>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.25135/acg.oc.158.2308.2887</relatedIdentifier>
  </relatedIdentifiers>
  <rightsList>
    <rights rightsURI="http://www.opendefinition.org/licenses/cc-by">Creative Commons Attribution</rights>
    <rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights>
  </rightsList>
  <descriptions>
    <description descriptionType="Abstract">&lt;p&gt;Peptides have low oral bioavailability, low plasma stability, and short circulation time; therefore, they are used in targeted strategies in cancer. In this study, according to in silico analysis, novel small peptide sequences, which are consist of three amino acid residues, with high binding capacity against the human FOLR1 surface molecule were obtained. Modeling studies were carried out to determine peptide sequences. RhB-K*FFF, RhB-K*WFE, and RhB-K*YDY peptides have been synthesized by using the Solid Phase Peptide Synthesis (SPPS) method, purified by Reverse Phase High-Performance Liquid Chromatography (RP-HPLC) and characterized by Liquid Chromatography-High Resolution Mass Spectrometry (LC-HRMS/MS) and proton nuclear magnetic resonance (1H-NMR). The purity of RhB-K*FFF, RhB-K*WFE, and RhB-K*YDY peptide are 96%, 95%, and 92%, respectively. Also, cell viability test was performed for the peptides. In our further study, the peptide with highest binding affinity will be conjugated with chemotherapeutic agent in order to improve its anti-cancer activity.&lt;/p&gt;</description>
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