TY - JOUR
TI - Comparative evaluation of four trityl-type amidomethyl polystyrene resins in Fmoc solid phase peptide synthesis
AU - Zikos, C.
AU - Livaniou, E.
AU - Leondiadis, L.
AU - Ferderigos, N.
AU - Ithakissios, D.S.
AU - Evangelatos, G.P.
JO - Journal of Peptide Science
PY - 2003
VL - 9
TODO - 7
SP - 419-429
PB - 
SN - 1075-2617, 1099-1387
TODO - 10.1002/psc.454
TODO - 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
TODO - 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.
ER -