Analysis of Cibacron blue F3G-A interaction with therapeutic proteins by MALDI-TOF mass spectrometry

Biomed Chromatogr. 2008 Sep;22(9):1001-7. doi: 10.1002/bmc.1019.

Abstract

The formation of the complexes between Cibacron blue F3G-A and two therapeutic proteins, recombinant human interferon-alpha2b and recombinant human growth hormone, was investigated. The method of time-resolved limited proteolysis coupled with MALDI-TOF mass spectrometry was used. The analysis of peptide maps revealed that A(17)HR(19) and L(20)HQLAFDTYQEFEEAYIPK(38) of hGH, and R(14)TLMLLAQMR(23) and D(33)RHDFGFPQEEFGNQFQK(50) of hIFN-alpha2b, exhibit affinity to Cibacron blue F3G-A.

MeSH terms

  • Coloring Agents / chemistry*
  • Drug Interactions
  • Human Growth Hormone / chemistry*
  • Humans
  • Interferon alpha-2
  • Interferon-alpha / chemistry*
  • Ligands
  • Peptides / chemistry*
  • Recombinant Proteins
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods*
  • Triazines / chemistry*

Substances

  • Coloring Agents
  • Interferon alpha-2
  • Interferon-alpha
  • Ligands
  • Peptides
  • Recombinant Proteins
  • Triazines
  • Human Growth Hormone
  • Cibacron Blue F 3GA