Cascade dissociations of peptide cation-radicals. Part 1. Scope and effects of amino acid residues in penta-, nona-, and decapeptides.
Cascade dissociations of peptide cation-radicals. Part 1. Scope and effects of amino acid residues in penta-, nona-, and decapeptides.
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DOI:
10.1007/s13361-012-0408-9
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发表时间:
2012-08
影响因子:
3.2
通讯作者:
Turecek, Frantisek
中科院分区:
文献类型:
--
作者:
Chung, Thomas W.;Hui, Renjie;Ledvina, Aaron;Coon, Joshua J.;Turecek, Frantisek
Amino acid residue-specific backbone and side-chain dissociations of peptide z ions in MS3 spectra were elucidated for over 40 pentapeptides with arginine C-terminated sequences of the AAXAR and AAHXR type, nonapeptides of the AAHAAXYAR and AAHAXAYAR type, and AAHAAXYAAR decapeptides. Peptide zn ions containing amino acid residues with readily transferrable benzylic or tertiary β-hydrogen atoms (Phe, Tyr, His, Trp, Val) underwent facile backbone cleavages to form dominant zn-2 or zn-3 ions. These backbone cleavages are thought to be triggered by a side-chain β-hydrogen atom transfer to the z ion Cα radical site followed by homolytic dissociation of the adjacent Cα—CO bond, forming zn-2 + HNCO cation-radicals that spontaneously dissociate by loss of HNCO. Amino acid residues that do not have readily transferrable β-hydrogen atoms (Gly, Ala) do not undergo the zn → zn-2 dissociations. The backbone cleavages compete with side-chain dissociations in z ions containing Asp and Asn residues. Side-chain dissociations are thought to be triggered by α-hydrogen atom transfers that activate the Cβ—Cγ or Cβ—heteroatom bonds for dissociations that dominate the MS3 spectra of z ions from peptides containing Leu, Cys, Lys, Met, Ser, Arg, Glu and Gln residues. The Lys, Arg, Gln, and Glu residues also participate in γ-hydrogen atom transfers that trigger other side-chain dissociations.
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