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Mass spectrometric investigations on Conus peptides

Mass spectrometric investigations on Conus peptides. Krishnamurthy, Thaiya; Prabhakaran, Muthuchidambaram; Long, S. Randolph (U.S. Edgewood RD&E Center, Aberdeen Proving Ground, Aberdeen, MD 21010-5423, USA). Toxicon, 34(11/12), 1345-1359 (English) 1996 Elsevier. CODEN: TOXIA6. ISSN: 0041-0101. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) Mol.There are some reagents with their cas registry numbers 129129-65-3 and 111317-91-0 are used in this study. masses and primary structure detn. of Conus peptides, such as a-, m- and w-conotoxins, conantokins and conopressins, were accurately measured by state-of-the-art mass spectrometric techniques using only 102 pmole quantities. Soft ionization of Conus peptides under electrospray, matrix-assisted laser desorption and continuous flow frit-FAB conditions produced their corresponding singly and multiply charged mol. ions which can be detected by mass spectrometric anal. The mol. masses of Conus peptides were obtained by the deconvolution of the multiply charged pseudo-mol. ions. Mixt. anal. without chromatog. sepn. can be accomplished by this approach. The ions formed during collision-induced dissocn. of either singly or multiply charged ions of any reduced and derivatized peptide provided the corresponding sequences of the amino acids. Preliminary investigations indicate that the developed techniques and procedures could be applied in order to characterize the peptides present in unknown Conus venoms from the Bay of Bengal region. .