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Type: Journal article
Title: Collision-induced fragmentations of the (M-H) parent anions of underivatized peptides: An aid to structure determination and some unusual negative ion cleavages
Author: Bowie, J.
Brinkworth, C.
Dua, S.
Citation: Mass Spectrometry Reviews, 2002; 21(2):87-107
Publisher: John Wiley & Sons Inc
Issue Date: 2002
ISSN: 0277-7037
Statement of
John H. Bowie, Craig S. Brinkworth and Suresh Dua
Abstract: This article describes the fundamental cleavage reactions of (M-H)(-) anions of underivatized peptides that contain up to 25 amino acid residues. The experimental observations of these cleavages have been backed up by molecular modeling, generally at the AM1 level of theory. The basic cleavages are the ubiquitous alpha- and beta-backbone cleavage reactions, which provide information similar to that of the B and Y + 2 cleavages of MH(+) ions of peptides. The residues Asp and Asn also effect cleavages of the backbone (called delta- and gamma-cleavages), by reactions initiated from side chain enolate anions, causing elimination reactions that cleave the backbone between the Asp (Asn) N bond;C backbone bond. Glu and Gln also direct analogous delta- and gamma-cleavages of the backbone, but in this case the processes are initiated by attack of the side chain CO(2) (-) (CONH(-)) to form a lactone (lactam). Ser and Thr residues undergo characteristic fragmentations of the side chain. These processes, losses of CH(2)O (Ser) and MeCHO (Thr), convert these residues into Gly. In larger peptides, Ser and Thr can effect two backbone cleavage reactions, called gamma- and epsilon -processes. The C-terminal CO(2) (-) (or CONH(-)) forms a hydrogen bond with the side chain OH (of Ser or Thr), placing the C-terminal residue in a position where it may affect S(N) (2) attack at the electrophilic backbone CH of Ser, with concomitant cleavage of the backbone. All of the above negative ion cleavages require the peptide backbone to be conformationally flexible. However, there is a backbone cleavage that requires the peptide to have an alpha-helical conformation in order for the two reacting centers to approach. This cleavage is illustrated for the Glu 23-initiated backbone cleavage at Ile 21 for the (M-H)(-) anion of the antimicrobial peptide caerin 1.1.
Keywords: peptides; electrospray spectra; negative ions; fragmentations; theoretical calculations
Rights: © 2002 Wiley Periodicals, Inc.
RMID: 0020022250
DOI: 10.1002/mas.10022
Published version:
Appears in Collections:Chemistry publications

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