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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 β cleavage: a joint experimental and theoretical study
Author(s) -
Brinkworth Craig S.,
Dua Suresh,
Bowie John H.
Publication year - 2002
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.630
Subject(s) - chemistry , amide , residue (chemistry) , terminal (telecommunication) , stereochemistry , organic chemistry , telecommunications , computer science
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 α cleavage ions (and to a lesser extent β 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 β′ ions, in order to distinguish them from standard β ions. Some β′ ions also fragment directly to some other β′ ions of smaller mass. The reaction coordinates of α,β and β′ backbone processes have been calculated at the HF/6‐31G*//AM1 level theory for simple model systems. The initial cyclisation step of the β′ 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. Copyright © 2002 John Wiley & Sons, Ltd.