Abstract
Summary New volatile peptide derivatives have been prepared by reduction of N-trifluoroacetyl, N-pentafluoropropionyl and N-heptafluorobutyryl oligopeptide methyl esters by lithium aluminum deuteride and subsequent O-trimethylsilylation. The resulting O-trimethylsilylated dideutero-perfluoroalkyl polyamino alcohols are shown to be the most volatile peptide derivatives hitherto known. Their mass spectra exhibit abundant and intensity-balanced sequence-determining ions as well as M-15 ions. These properties permit the determination of the sequence of oligopeptides in the extremely complex mixtures which result from the hydrolysis of polypeptides or proteins (as little as 1 nanomole of a particular peptide can be detected).
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