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Tandem mass spectrometry analysis of synthetic opioid peptide analogs
Author(s) -
Tseng JihLie,
Yan Lin,
Fridland Genevieve H.,
Desiderio Dominic M.
Publication year - 1995
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290090404
Subject(s) - chemistry , tandem mass spectrometry , chromatography , mass spectrometry , tandem , peptide , protein mass spectrometry , isobaric labeling , combinatorial chemistry , biochemistry , materials science , composite material
Five synthetic opioid peptides that were designed to have specific opioid receptor‐binding properties were studied by low energy collision‐induced dissociation (CID) tandem mass spectrometry (MS/MS). The MS/MS data are required for the analysis of those peptides in ovine plasma in a study to determine the placental transfer of the peptide to the fetus. The synthetic enkephalin‐related peptides were: Tyr‐D‐Arg‐Phe‐Lys‐NH 2 , (DALDA), N,N‐diallyl‐Tyr‐Aib‐Aib‐Phe‐Leu‐OH, (ICI 174,864), Tyr‐D‐Thr‐Gly‐Phe‐Leu‐Thr, (DTLET),. Liquid secondary ion mass spectrometry (LSIMS) was used for sample desorption‐ionization, and a hybrid (E 1 BE 2 qQ) tandem mass spectrometer was used to collect the product‐ion spectra. A protonated molecule ion, [M + H] + , was observed for each peptide. Amino acid sequence‐determining fragment ions were produced by CID and collected by MS/MS for the three linear peptides, and also for the two disulfide‐bond‐containing peptides in their unreduced and dithiothreitol (DTT)‐reduced forms. The detection level for the [M + H] + ion of DTLET was ca . 3 pmol; and the stabilities of the CTAP and ICI analogs in plasma were studied.