GENERAL APPROACH TO THE QUANTITATION OF SYNTHETIC EFFICIENCY IN SOLID-PHASE PEPTIDE SYNTHESIS AS A FUNCTION OF CHAIN LENGTH.

Article abstract of DOI:10.1021/ja00337a033

A model peptide, Leu-Ala-Gly-Val, was synthesized by solid-phase methods at increasing distnces from a 1% cross-linked polystyrene resin support. The efficiency of the synthesis was evaluated by quantitatively measuring the amounts of the deletion peptides Leu-Ala-Val and Leu-Gly-Val that were produced during the synthesis of the tetrapeptide. By inserting an oxymethylphenylacetyl group between this test peptide and the peptide chains used to provide spacers from the support, it was possible to selectively evaluate the quality of the tetrapeptide without interference by the spacer. Low and constant levels of deletion peptides were found. No significant effect of distance from the support or of peptide loading on the synthetic efficiency could be detected up to a chain length of 60 residues and a peptide-to-resin weight ratio of 4:1.