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Type: Journal article
Title: Backbone cleavages of [M - H]- anions of peptides. Cyclisation of citropin 1 peptides involving reactions between the C-terminal [CONH]- residue and backbone amide carbonyl groups. A new type of b cleavage: a joint experimental and theoretical study
Author: Brinkworth, C.
Dua, S.
Bowie, J.
Citation: Rapid Communications in Mass Spectrometry, 2002; 16(7):713-721
Publisher: John Wiley & Sons Ltd
Issue Date: 2002
ISSN: 0951-4198
Statement of
Craig S. Brinkworth, Suresh Dua, John H. Bowie
Abstract: This paper reports the study of backbone cleavages in the collision-induced negative-ion mass spectra of the [M - H](-) anions of some synthetic modifications of the bioactive amphibian peptide citropin 1 (GLFDVIKKVASVIGGL-NH(2)). The peptides chosen for study contain no amino acid residues which could effect facile side-chain cleavage, i.e. Ser (-CH(2)O, side-chain cleavage) and Asp (-H(2)O) are replaced by Ala or Lys. We expected that such peptides should exhibit standard and pronounced peaks due to alpha cleavage ions (and to a lesser extent beta cleavage ions) in their collision-induced negative-ion spectra. This expectation was realised, but the spectra also contained peaks formed by a new series of cleavage anions. These are produced following cyclisation of the C-terminal CONH(-) moiety at carbonyl functions of amide groups along the peptide backbone; effectively transferring the NH of the C-terminal CONH(-) group to other amino acid residues. We have called the product anions of these processes beta' ions, in order to distinguish them from standard beta ions. Some beta' ions also fragment directly to some other beta' ions of smaller mass. The reaction coordinates of alpha,beta and beta' backbone processes have been calculated at the HF/6-31G*//AM1 level theory for simple model systems. The initial cyclisation step of the beta' sequence is barrierless and exothermic. Subsequent steps have a maximum barrier of +40 kcal mol(-1), with the overall reaction being endothermic by some 30 kcal mol(-1) at the level of theory used. These calculations take no account of the complexity of the conformationally flexible peptide system, and it is surprising that each of the two reacting centres can 'find' each other in such a large system.
Description: The definitive version may be found at
RMID: 0020020126
DOI: 10.1002/rcm.630
Published version:
Appears in Collections:Chemistry publications

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