Delineating protein-protein interactions via biomolecular interaction analysis-mass spectrometry

Dobrin Nedelkov, Randall W. Nelson

Research output: Contribution to journalArticlepeer-review

23 Scopus citations


The utility of biomolecular interaction analysis-mass spectrometry (BIA/MS) in screening for protein-protein interactions was explored in this work. Experiments were performed in which proteins served as ligands for screening of possible interactions with other proteins from human plasma and urine. The proteins utilized were beta-2-microglobulin, cystatin C (cysC), retinol binding protein (RBP), transthyretin (TTR), alpha-1-microglobulin, C-reactive protein, transferrin and papain. The immobilization of functionally active proteins was confirmed via interactions with antibodies to the corresponding proteins. Various dilutions of human urine and plasma were injected over the protein-derivatized surfaces. It was observed that the urine injections generally yielded smaller SPR responses than those observed after the plasma injections. The BIA/MS experiments did not reveal novel protein-protein interactions, although several established interactions (such as those between RBP and TTR, and cysC and papain) were validated. Few protein ligand deficiencies (such as truncations) leading to false negative and false positive BIA/MS results were also discovered.

Original languageEnglish (US)
Pages (from-to)9-14
Number of pages6
JournalJournal of Molecular Recognition
Issue number1
StatePublished - Jan 2003


  • BIA/MS
  • Biosensor
  • Chip
  • Ligands
  • MALDI-TOF mass spectrometry
  • Protein-protein interactions
  • SPR

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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