Diagonal chromatographic selection of cysteinyl peptides modified with benzoquinones.
The derivatization of cysteine-containing peptides with benzoquinone compounds is rapid, quantitative and specific in acidic media. The conversion of cysteines into hydrophobic benzoquinone-adducted residues in peptides is used here to alter the chromatographic properties of cysteinyl peptides during liquid chromatography separation. The benzoquinone derivatization is shown to allow the accurate selection of cysteine-containing peptides of bovine serum albumin tryptic digest by diagonal reversed-phase chromatography, which consists of one primary and a series of secondary identical liquid chromatographic separations, before and after a cysteinyl-targeted modification of the peptides by benzoquinone compounds.
Dayon
Loïc
L
Laboratoire d'Electrochimie Physique et Analytique, Ecole Polytechnique Fédérale de Lausanne (EPFL), Station 6, 1015 Lausanne, Switzerland.
Girault
Hubert H
HH
D000595:Amino Acid Sequence; D016227:Benzoquinones / Q000737:chemistry*; D002853:Chromatography, Liquid / Q000379:methods; D003545:Cysteine / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis* / Q000737:chemistry; D040901:Proteomics / Q000379:methods*; D012710:Serum Albumin, Bovine / Q000032:analysis / Q000737:chemistry / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D016227:Benzoquinones; D010455:Peptides; D012710:Serum Albumin, Bovine; C004532:quinone; D014357:Trypsin; D003545:Cysteine