@article{3022760, title = "Comparative evaluation of four trityl-type amidomethyl polystyrene resins in Fmoc solid phase peptide synthesis", author = "Zikos, C. and Livaniou, E. and Leondiadis, L. and Ferderigos, N. and Ithakissios, D.S. and Evangelatos, G.P.", journal = "Journal of Peptide Science", year = "2003", volume = "9", number = "7", pages = "419-429", issn = "1075-2617, 1099-1387", doi = "10.1002/psc.454", keywords = "amino acid; dichloromethane; fluorene derivative; polystyrene derivative; proline; resin; tetrapeptide; thymosin beta4, acidity; amino terminal sequence; article; carboxy terminal sequence; chemical bond; comparative study; controlled study; molecular stability; peptide synthesis; priority journal; protein purification; sensitivity analysis; solid, Molecular Structure; Oligopeptides; Polystyrenes; Resins, Synthetic", abstract = "Four trityl-type (i.e. non-substituted trityl-, o-Cl-trityl-, o-F-trityl- and p-CN-trityl-) amidomethyl polystyrene resins were evaluated comparatively, in terms of the stability of the trityl-ester bond in slightly acidic dichloromethane solutions, and the p-CN-trityl-amidomethyl polystyrene resin was found to be the most stable of them. The above resins were applied, in parallel with Wang benzyl-type resin, well known for its stability in mild acidic conditions, to the Fmoc solid phase synthesis of the 43-amino acid residue long bioactive peptide thymosin beta-4. Independent of their differences in acid sensitivity, the resins seemed to function equally well under the conditions used, since pure thymosin beta-4 was obtained with a final yield of approximately 30% from each resin. The trityl-type amidomethyl polystyrene resins were also applied, in parallel with the Wang resin, to the Fmoc solid phase synthesis of a bioactive peptide containing proline at its C-terminus, i.e. the N-terminal tetrapeptide of thymosin beta-4, AcSDKP. In this case, the best yield (87%) was obtained with the o-Cl-trityl-amidomethyl polystyrene resin, which may be the resin of choice, of those studied, for the Fmoc solid phase peptide synthesis. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd." }