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dc.contributor.authorMalkinson, John P.
dc.contributor.authorZloh, Mire
dc.contributor.authorKadom, Mohanad
dc.contributor.authorErrington, Rachel J.
dc.contributor.authorSmith, Paul J.
dc.contributor.authorSearcey, Mark
dc.identifier.citationMalkinson , J P , Zloh , M , Kadom , M , Errington , R J , Smith , P J & Searcey , M 2003 , ' Solid-phase synthesis of the cyclic peptide portion of chlorofusin, an inhibitor of p53-MDM2 interactions ' , Organic letters , vol. 5 , no. 26 , pp. 5051-4 .
dc.identifier.otherPURE: 1458384
dc.identifier.otherPURE UUID: f597300b-98c4-4ea7-a49e-8987cea530b1
dc.identifier.otherPubMed: 14682762
dc.identifier.otherScopus: 0346025402
dc.description.abstractThe first solid-phase synthesis of the chlorofusin peptide is described. The synthesis involved side-chain immobilization of N(alpha)-Fmoc-Asp-ODmab. Synthesis of the linear peptide, initially incorporating racemic Ade8 and unsubstituted ornithine in place of the chromophore-bearing residue, was followed by cyclization on resin and peptide release to give a mixture of diastereomers. Resynthesis identified (by HPLC) the second isomer as analogous to the natural product. Initial biological assays, using an immunofluorescence method, suggest that the compounds are not cytotoxic but do not inhibit the p53/mdm2 interaction. [structure: see text]en
dc.relation.ispartofOrganic letters
dc.titleSolid-phase synthesis of the cyclic peptide portion of chlorofusin, an inhibitor of p53-MDM2 interactionsen
dc.contributor.institutionDepartment of Pharmacy
dc.contributor.institutionMedicinal and Analytical Chemistry
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.description.statusPeer reviewed
dc.relation.schoolSchool of Life and Medical Sciences
rioxxterms.typeJournal Article/Review

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