1 Ocak 2018 Dergi makalesi Açık Erişim

Timur, Selin Seda; Yalcin, Goezde; Cevik, Ozge; Andac, Cenk; Gursoy, R. Neslihan

Dublin Core

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  <dc:creator>Timur, Selin Seda</dc:creator>
  <dc:creator>Yalcin, Goezde</dc:creator>
  <dc:creator>Cevik, Ozge</dc:creator>
  <dc:creator>Andac, Cenk</dc:creator>
  <dc:creator>Gursoy, R. Neslihan</dc:creator>
  <dc:date>2018-01-01</dc:date>
  <dc:description>Recent studies in tumor homing peptides have shown the specificity of LyP-1 (CGNKRTRGC) to tumor lymphatics. In this present work, we evaluated the possible interactions between cyclic LyP-1 and its receptor, p32, with molecular dynamics and docking studies in order to lead the design of novel LyP-1 derivatives, which could bind to p32 more effectively and perform enhanced antitumor effect. The total binding enthalpy energies have been obtained by MM-PBSA thermodynamic computations and the favorability of p32.LyP-1 complex in water has been shown by explicit water MD computations. The last 30ns of molecular dynamics trajectory have shown the strong interaction of LyP-1 with the inner surface chains of p32, especially with chains B and C. ALA-SCAN mutagenesis studies have indicated the considerable influence of Asn3, Lys4, Arg5, and Arg7 amino acid residues on the specific binding of LyP-1. Within the knowledge of the critical role of p32 receptor in cancer cell metabolism, this study can lead to further developments in anticancer therapy by targeting p32 with LyP-1 derivatives as active targeting moiety. This data can also be applied for the development of new drug delivery systems in which LyP-1 can be used for its targeting and anticancer properties.</dc:description>
  <dc:identifier>https://aperta.ulakbim.gov.trrecord/29735</dc:identifier>
  <dc:identifier>oai:zenodo.org:29735</dc:identifier>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>http://www.opendefinition.org/licenses/cc-by</dc:rights>
  <dc:source>JOURNAL OF BIOMOLECULAR STRUCTURE &amp; DYNAMICS 36(5) 1134-1144</dc:source>
  <dc:title>Molecular dynamics, thermodynamic, and mutational binding studies for tumor-specific LyP-1 in complex with p32</dc:title>
  <dc:type>info:eu-repo/semantics/article</dc:type>
  <dc:type>publication-article</dc:type>
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