High-Affinity Capture of Proteins by Diamond Nanoparticles for Mass Spectrometric Analysis
Citations Over TimeTop 10% of 2004 papers
Abstract
Carboxylated/oxidized diamond nanoparticles (nominal size 100 nm) exhibit exceptionally high affinity for proteins through both hydrophilic and hydrophobic forces. The affinity is so high that proteins in dilute solution can be easily captured by diamonds, simply separated by centrifugation, and directly analyzed by matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS). No preseparation of the adsorbed molecules from diamonds is required for the mass spectrometric analysis. Compared to conventional MALDI-TOF-MS, an enhancement in detection sensitivity by more than 2 orders of magnitude is achieved for dilute solution containing cytochrome c, myoglobin, and albumin because of preconcentration of the probed molecules. The lowest concentration detectable is 100 pM for a 1-mL solution. Aside from the enhanced sensitivity, the overall performance of this technique does not show any sign of deterioration for highly contaminated protein solutions, and furthermore, no significant peak broadening and band shift were observed in the mass spectra. The promise of this new method for clinical proteomics research is demonstrated with an application to human blood serum.
Related Papers
- → Blue Myoglobin Reconstituted with an Iron Porphycene Shows Extremely High Oxygen Affinity(2002)123 cited
- → Met-myoglobin formation, accumulation, degradation, and myoglobin oxygenation monitoring based on multiwavelength attenuance measurement in porcine meat(2016)13 cited
- → A Histological Study of Myoglobin in Developing Muscle of the Pig(1970)7 cited
- The Diffusion Coefficient of Myoglobin in Muscle Homogenate(1968)