Aggregation of resin-bound peptides during solid-phase peptide synthesis. Prediction of difficult sequences.
Nonrandom incomplete aminoacylation of a pendent peptide chain on an insoluble polymeric support during solid-phase peptide synthesis is sequence-dependent and is caused by aggregation of peptide chains, manifested by a decreased swelling capacity. The volume of the swollen peptidyl-resin after each coupling during the syntheses of 87 sequence unrelated peptides was measured, and for each amino acid an aggregation parameter, <Pa>, was derived that reflects the propensity of the swollen volume of peptidyl-resin to decrease during peptide synthesis. These aggregation parameters were used to predict potentially difficult sequences.
Krchnák
V
V
Research Institute for Feed Supplements and Veterinary Drugs, Jílové, Prague, Czeck Republic.
Flegelová
Z
Z
Vágner
J
J
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D011485:Protein Binding; D012116:Resins, Plant / Q000737:chemistry*
D010455:Peptides; D012116:Resins, Plant