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

Biomolecular interaction analysis mass spectrometry (BIA/MS) is a two-dimen sional chip-based analytical technique geared toward quantitative and quali tative analysis of small volumes of biological samples. interactions betwee n 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 a nalysis of the analyte(s) affinity-retained on the sensor surface. In this work, MAIMS was used in the detection of a number of protein biomarkers fro m human urine. Small volumes of human urine were analyzed for cystatin C, b eta (2)-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 sen sor chip configuration. Furthermore, RBP was analyzed separately from both urine and plasma samples. Results indicate that BIA/MS can be used successf ully in rapid screening of a number of urinary proteins indicated as putati ve biological markers for renal dysfunction. (C) 2001 by the National Kidne y Foundation, Inc.