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Convergent solid‐phase and solution approaches in the synthesis of the cysteine‐rich Mdm2 RING finger domain
Author(s) -
Vasileiou Zoe,
Barlos Kostas,
Gatos Dimitrios
Publication year - 2009
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1182
Subject(s) - cysteine , solid phase synthesis , ring (chemistry) , ring finger , ring finger domain , chemistry , phase (matter) , domain (mathematical analysis) , combinatorial chemistry , biophysics , biochemistry , mathematics , zinc finger , biology , organic chemistry , mathematical analysis , peptide , transcription factor , gene , enzyme
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. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd.