Analysis of human urine protein biomarkers via biomolecular interaction analysis mass spectrometry

Dobrin Nedelkov, Randall W. Nelson

Research output: Contribution to journalArticle

46 Scopus citations

Abstract

Biomolecular interaction analysis mass spectrometry (BIA/MS) is a two-dimensional chip-based analytical technique geared toward quantitative and qualitative analysis of small volumes of biological samples. Interactions between surface-immobilized ligands and solute-borne analytes are quantitatively viewed in real time through surface plasmon resonance sensing, followed by qualitative matrix-assisted laser desorption/ionization time-of-flight MS analysis of the analyte(s) affinity-retained on the sensor surface. In this work, BIA/MS was used in the detection of a number of protein biomarkers from human urine. Small volumes of human urine were analyzed for cystatin C, β2-microglobulin, urinary protein 1, and retinol-binding protein (RBP). Multiaffinity sensor surfaces were created to simultaneously and rapidly detect all four proteins in a single BIA/MS analysis on a two-flow cell sensor chip configuration. Furthermore, RBP was analyzed separately from both urine and plasma samples. Results indicate that BIA/MS can be used successfully in rapid screening of a number of urinary proteins indicated as putative biological markers for renal dysfunction.

Original languageEnglish (US)
Pages (from-to)481-487
Number of pages7
JournalAmerican Journal of Kidney Diseases
Volume38
Issue number3
DOIs
StatePublished - Jan 1 2001

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Keywords

  • Biosensor
  • Mass spectrometry (MS)
  • Matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF)
  • Renal dysfunction
  • Surface plasmon resonance (SPR)
  • Urinary biomarkers

ASJC Scopus subject areas

  • Nephrology

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