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MALDI mass spectrometry of dye-peptide and dye-protein complexes.
Journal article

MALDI mass spectrometry of dye-peptide and dye-protein complexes.

  • Salih B Department of Chemistry, ETH Zentrum, Zürich, Switzerland.
  • Zenobi R
  • 1998-05-07
Published in:
  • Analytical chemistry. - 1998
Adrenocorticotropic Hormone
Aniline Compounds
Benzenesulfonates
Binding Sites
Bombesin
Coloring Agents
Cytochrome c Group
Insulin
Melitten
Peptides
Proteins
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Substance P
Triazines
Ubiquitins
English Immobilized sulfonate dyes are widely used for protein separation and purification, but the mode of interaction between the dye molecules and the proteins is largely unknown. Here we show that specific noncovalent dye-protein and dye-peptide complexes can be observed using MALDI mass spectrometry. We prove that the interaction is prodominantly electrostatic and that it involves protonated sites of the peptides and proteins, including the NH2 terminus, and deprotonated SO3 groups of the dyes. Furthermore, we show that MALDI-MS of such complexes with a nonacidic matrix, p-nitro-aniline, can be used to determine the number of accessible basic sites of a protein or peptide in its folded structure. Our results are in good agreement with measurements of the same property done with electrospray ionization.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/222618
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