Abstract
High-resolution electrospray ionization (ESI) quadrupole time-of-flight and ion trap tandem mass spectrometry has been used to distinguish the positional isomers of a new class of N-blocked hybrid peptides containing repeats of the amino acids, L-Ala-γ 4Caa (l)/γ 4Caa(l)-L-Ala [Caa(l) = Carbo (lyxose) amino acid, derived from D-mannose]. Both MS/MS and MS3 of protonated isomeric peptides produce characteristic fragmentation involving the peptide backbone, Boc-group, and the side-chain. It is interesting to observe that the abundant y +n ions are formed when the corresponding amide −NH does not participate in the helical structures in solution phase and relatively low abundance y +n ions resulted when the amide −NH involves in the H-bonding. Thus, it was possible to identify the amide −NH hydrogens that participate in the helical structures through H-bonding in solution phase. Further, negative ion ESI MS/MS has also been found to be useful for differentiating these isomeric peptide acids.
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Published online January 16, 2007
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Reddy, P.N., Srinivas, R., Kumar, M.R. et al. Positive and negative ion electrospray tandem mass spectrometry (ESI MS/MS) of boc-protected peptides containing repeats of L-Ala-γ 4Caa/γ 4Caa-L-Ala: Differentiation of some positional isomeric peptides. J Am Soc Mass Spectrom 18, 651–662 (2007). https://doi.org/10.1016/j.jasms.2006.12.005
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DOI: https://doi.org/10.1016/j.jasms.2006.12.005