A new, improved technique for automated sequencing of non-polar peptides

A method for the automated sequential degradation of non-polar peptides is reported. Both the polarity and film-forming properties of these peptides are increased by the attachment of 2-amino-1,5 napthalene disulfonic acid to the C-terminal residue via a water-soluble carbodiimide. The sequences of three individual peptides modified by the procedure are reported with high yields while these same peptides could not be successfully sequenced if no modification was made.