Effect of urea surface modification and photocatalytic cleaning on surface-assisted laser desorption ionization mass spectrometry with amorphous TiO2 nanoparticles

✍ Scribed by Takehiro Watanabe; Koji Okumura; Hideya Kawasaki; Ryuichi Arakawa

• Publisher: John Wiley and Sons
• Year: 2009
• Tongue: English
• Weight: 318 KB
• Volume: 44
• Category: Article
• ISSN: 1076-5174
• DOI: 10.1002/jms.1628

✦ Synopsis

Abstract

We have investigated the effect of urea surface modification and the photocatalytic cleaning on surface‐assisted laser desorption ionization mass spectrometry (SALDI‐MS) with amorphous TiO~2~ nanoparticles for the reduction of the background noise and the improvement of the sensitivity. In the use of nanoparticles of high surface area, chemical background signals arising from ambient environments and organic contaminants can frequently be serious problems below 500 Da, possibly reducing the advantages of the matrix‐free approach. In this study, removal of contaminants and enhanced SALDI efficiency were easily achieved with UV irradiation via the photocatalyst effect of TiO~2~ before SALDI‐MS measurements. The surface cleaning achieved by the UV photocatalytic procedure reduced the background noise and increased the peak intensities of peptides. In addition, we found that urea surface modification of TiO~2~ nanoparticles increased the performance of the TiO~2~‐SALDI‐MS. (1) The urea‐surface modification of TiO~2~ made it possible to produce proton‐adduct forms without citrate buffer, resulting in low background noises below 500 Da, in contrast to the essential use of a citrate buffer in the bare TiO~2~‐SALDI‐MS. (2) The detection sensitivity of angiotensin I increased to 0.3 fmol with the urea‐surface modification, as compared to the use of bare TiO~2~ nanoparticles (6 fmol). The urea‐TiO~2~ could ionize proteins of more than 20 000 Da such as trypsinogen (600 fmol). (3) The urea modification of TiO~2~ had the advantage of selective detection of phosphopeptides without sample clean up, or prefractionation in tryptic digest products of bovine hemoglobin. Copyright © 2009 John Wiley & Sons, Ltd.