title: Difficult couplings in stepwise solid phase peptide synthesis: predictable or just a guess?
abstract: Stepwise solid phase peptide synthesis, Fmoc-approach, of 88 peptides varying in length from 4 to 24 amino acid residues was performed using a uniform procedure for coupling, monitoring and deprotection steps. The data of 696 couplings have been incorporated into a computer programme in order to study whether the degree of coupling can be predicted. Parameters studied are the nature of the amino acid to be coupled, the amino acid to be acylated and the length of the growing peptide chain. Using this information, prediction of "good" or "difficult" sequences, that is, peptides that can be synthesized without appreciable repeated couplings or the opposite, seems possible.
authors.affiliation: Organon Scientific Development Group, Oss, The Netherlands.
authors.forename: W J
authors.initials: WJ
authors.lastname: van Woerkom
authors.forename: J W
authors.initials: JW
authors.lastname: van Nispen
mesh_terms: D000215:Acylation; D000596:Amino Acids; D003201:Computers; D005449:Fluorenes; D005755:Gastrins / Q000037:antagonists & inhibitors; D009842:Oligopeptides / Q000138:chemical synthesis*; D010455:Peptides / Q000138:chemical synthesis*; D012117:Resins, Synthetic / Q000737:chemistry; D012984:Software
chemical_list: D000596:Amino Acids; D005449:Fluorenes; D005755:Gastrins; D009842:Oligopeptides; D010455:Peptides; D012117:Resins, Synthetic; C008530:minigastrin