首页 | 本学科首页   官方微博 | 高级检索  
   检索      


Fast atom bombardment mass spectrometry analysis of opioid peptides
Authors:C Dass  D M Desiderio
Institution:1. Smap UA-UVA-CSIC, Parque Científico Universidad de Valladolid, Paseo de Belén, s/n, 47011 Valladolid, Spain;2. Dept. Física Aplicada, Facultad de Ciencias, Universidad de Valladolid, Paseo de Belén, 7, 47011 Valladolid, Spain;3. Instituto de Ciencia y Tecnología de Polímeros, CSIC, Juan de la Cierva 3, 28006 Madrid, Spain;1. University of Valladolid, Valladolid, Spain;4. Ohio University, Athens, OH, USA;5. University of Burgos, Burgos, Spain
Abstract: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.
Keywords:
本文献已被 ScienceDirect 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号