Fast atom bombardment mass spectrometry analysis of opioid peptides.
Positive and negative ion fast atom bombardment mass spectrometries have been used to determine the amino acid sequence-determining fragment ion information of opioid peptides containing from 5 to 10 amino acid residues. The opioids investigated include several enkephalins, dynorphin A fragments 1-7 through 1-10, and alpha- and beta-neoendorphins. Data obtained in the two ionization polarities provide complementary information and exhibit the C-terminal- and the N-terminal-containing amino acid sequence-determining fragment ions that are formed by cleavage of the bond between the carbonyl group and the alpha-carbon (-CHR-CO-), the peptide amide bond (-CO-NH-), and the amino-alkyl (-NH-CHR-) bond. The C-terminal sequence ions are dominant in the positive ion mode, whereas the C-terminal and N-terminal ions are equally important in the negative ion mode. Detection limits for full mass scans extend down to the picomole range. The apparent role of hydrophobicity of the amino acid residues on the fragmentation characteristics of the peptide is discussed.
D000595:Amino Acid Sequence; D004399:Dynorphins / Q000032:analysis; D004563:Electrochemistry; D004723:Endorphins / Q000032:analysis*; D004745:Enkephalins / Q000032:analysis; D013058:Mass Spectrometry / Q000379:methods
D004723:Endorphins; D004745:Enkephalins; D004399:Dynorphins