Differentiation of isomeric amino acid residues in proteins and peptides using mass spectrometry.
Characterization and differentiation of isomers in biological macromolecules using mass spectrometry is one of the most significant challenges facing scientists in the field. The capability of high-resolution MS instruments along with the development of new fragmentation methods now provides the ability to indirectly differentiate between some isomers. This ability has enabled mass spectrometry to evolve into a multidisciplinary technique incorporating areas such as pharmaceutical research, proteomics, polymer science, medicine, environmental chemistry, and recently archeology. This article aims to review recent developments in mass spectrometry methodologies in the identification of structural and spatial isomers in biological macromolecules, such as aspartic acid and isoaspartic acid (Asp/IsoAsp), leucine and isoleucine (Leu/Ile), glutamic acid and γ-glutamic acid, and D/L enantiomers.
Department of Chemistry, University of Warwick, Coventry, UK.
Pilar Perez
PP
Hurtado
Peter B
PB
O'Connor
D000818:Animals; D001224:Aspartic Acid / Q000032:analysis*; D018698:Glutamic Acid / Q000032:analysis*; D006801:Humans; D026581:Isoaspartic Acid / Q000032:analysis; D007532:Isoleucine / Q000032:analysis; D007536:Isomerism; D007930:Leucine / Q000032:analysis*; D013058:Mass Spectrometry / Q000379:methods*; D010455:Peptides / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*
D026581:Isoaspartic Acid; D010455:Peptides; D011506:Proteins; D007532:Isoleucine; D001224:Aspartic Acid; D018698:Glutamic Acid; D007930:Leucine