AI Article Synopsis
- Detecting D-amino acid residues in natural peptides is difficult because they don't change the molecular mass, complicating identification by standard methods.
- This article is notable for being the first to use matrix-assisted laser desorption/ionization (MALDI) for distinguishing and quantifying peptide isomers.
- The researchers examined synthetic hepta- and decapeptides, including both all-L sequences and isomers with D-residues in various locations, to assess this technique.
Article Abstract
Detection of a D-amino acid residue in natural peptides by mass spectrometry remains a challenging task, as this post-translational modification does not induce any change in molecular mass. To our knowledge, the present article is the first report using matrix-assisted laser desorption/ionization (MALDI) for the discrimination and the quantification of peptide isomers. In this work, we used synthetic hepta- and decapeptides of biological relevance and their isomers. All-L sequences and some isomers containing a D-residue in various positions were analyzed.
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| http://dx.doi.org/10.1021/ac9002886 | DOI Listing |
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