d-Amino Acid Detection in Peptides by MALDI-TOF-TOF

• Published in: Analytical chemistry (Washington) Vol. 81; no. 11; pp. 4389 - 4396
• Main Authors: Sachon, Emmanuelle, Clodic, Gilles, Galanth, Cécile, Amiche, Mohamed, Ollivaux, Céline, Soyez, Daniel, Bolbach, Gérard
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01.06.2009
• Subjects: Amino Acid Sequence; Amino Acids; Amino Acids - analysis; Amino Acids - chemistry; Analytical chemistry; Biochemistry, Molecular Biology; Carrier Proteins; Carrier Proteins - analysis; Chemical compounds; Chemistry; Desorption; Exact sciences and technology; Invertebrate Hormones; Invertebrate Hormones - analysis; Isomerism; Life Sciences; Mass spectrometry; Opioid Peptides; Opioid Peptides - analysis; Peptides; Peptides - analysis; Peptides - chemistry; Spectrometric and optical methods; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods; Peptides; Time of flight method; Residue; Aminoacid; Matrix assisted laser desorption ionization; Mass spectrometry; Quantitative analysis; Isomer
• ISSN: 0003-2700; 1520-6882
• DOI: 10.1021/ac9002886

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.