title: Convergent solid-phase and solution approaches in the synthesis of the cysteine-rich Mdm2 RING finger domain.
abstract: The RING finger domain of the Mdm2, located at the C-terminus of the protein, is necessary for regulation of p53, a tumor suppressor protein. The 48-residues long Mdm2 peptide is an important target for studying its interaction with small anticancer drug candidates. For the chemical synthesis of the Mdm2 RING finger domain, the fragment condensation on solid-phase and the fragment condensation in solution were studied. The latter method was performed using either protected or free peptides at the C-terminus as the amino component. Best results were achieved using solution condensation where the N-component was applied with the C-terminal carboxyl group left unprotected. The developed method is well suited for large-scale synthesis of Mdm2 RING finger domain, combining the advantages of both solid-phase and solution synthesis.
authors.affiliation: Department of Chemistry, University of Patras, Patras, Greece.
authors.forename: Zoe
authors.initials: Z
authors.lastname: Vasileiou
authors.forename: Kostas
authors.initials: K
authors.lastname: Barlos
authors.forename: Dimitrios
authors.initials: D
authors.lastname: Gatos
mesh_terms: D000595:Amino Acid Sequence; D003545:Cysteine / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry / Q000235:genetics; D051736:Proto-Oncogene Proteins c-mdm2 / Q000138:chemical synthesis / Q000737:chemistry / Q000235:genetics; D054829:RING Finger Domains; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry / Q000235:genetics
chemical_list: D010446:Peptide Fragments; D016159:Tumor Suppressor Protein p53; D051736:Proto-Oncogene Proteins c-mdm2; D003545:Cysteine