Study of non-covalent complexation between catechin derivatives and peptides by electrospray ionization mass spectrometry

J Mass Spectrom. 2002 Jun;37(6):609-16. doi: 10.1002/jms.321.


The recent development of electrospray ionization mass spectrometry (ESI-MS) has allowed its use to study molecular interactions driven by non-covalent forces. ESI-MS has been used to detect non-covalent complexes between proteins and metals, ligands and peptides and interactions involving DNA, RNA, oligonucleotides and drugs. Surprisingly, the study of the interaction between polyphenolic molecules and peptides/proteins is still an area where ESI-MS has not benefited. With regard to the important influence of these interactions in the biological and food domains, ESI-MS was applied to the detection and the characterization of soluble polyphenol-peptide complexes formed in model solution. The ability to observe and monitor the weak interactions involved in such macromolecular complexation phenomena was demonstrated for monomeric and dimeric flavonoid molecules (catechin-derived compounds) largely encountered in plants and plant derived products. Intact non-covalent polyphenol-peptide complexes were observed by ESI-MS using different experimental conditions. Utilizing mild ESI interface conditions allowed the detection of 1 : 1 polyphenol-peptide complexes in all tested solutions and 2 : 1 complexes for the dimers and galloylated polyphenols (flavanols). These results show that there is a preferential interaction between polymerized and/or galloylated polyphenols and peptide compared with that between monomeric polyphenols and peptides. Thus, ESI-MS shows potential for the study of small polyphenolic molecule-peptide interactions and determination of stoichiometry.

MeSH terms

  • Amino Acid Sequence
  • Catechin / analogs & derivatives*
  • Catechin / chemistry*
  • Dimerization
  • Food Analysis
  • Macromolecular Substances
  • Molecular Sequence Data
  • Peptide Fragments / chemistry*
  • Peptides / chemistry*
  • Proline-Rich Protein Domains
  • Solutions
  • Spectrometry, Mass, Electrospray Ionization*


  • Macromolecular Substances
  • Peptide Fragments
  • Peptides
  • Solutions
  • gallocatechin gallate
  • Catechin
  • epicatechin gallate
  • epigallocatechin gallate
  • gallocatechol