| Autor: |
Aguedo J; Institute of Chemistry, Slovak Academy of Sciences, 841 04 Bratislava, Slovakia., Vojs M; Institute of Electronics and Photonics, Faculty of Electrical Engineering and Information Technology, Slovak University of Technology, 841 04 Bratislava, Slovakia., Vrška M; Institute of Electronics and Photonics, Faculty of Electrical Engineering and Information Technology, Slovak University of Technology, 841 04 Bratislava, Slovakia., Nemcovic M; Centre of Excellence for Glycomic, Slovak Academy of Sciences, 841 04 Bratislava, Slovakia., Pakanova Z; Centre of Excellence for Glycomic, Slovak Academy of Sciences, 841 04 Bratislava, Slovakia., Dragounova KA; FZU-Institute of Physics, Czech Academy of Sciences, Cukrovarnická 10, 162 00 Prague, Czech Republic., Romanyuk O; FZU-Institute of Physics, Czech Academy of Sciences, Cukrovarnická 10, 162 00 Prague, Czech Republic., Kromka A; FZU-Institute of Physics, Czech Academy of Sciences, Cukrovarnická 10, 162 00 Prague, Czech Republic., Varga M; Institute of Electrical Engineering, Slovak Academy of Sciences, 841 04 Bratislava, Slovakia., Hatala M; Department of Graphic Arts Technology and Applied Photochemistry, Faculty of Chemical and Food Technology, Slovak University of Technology, 812 37 Bratislava, Slovakia., Marton M; Institute of Electronics and Photonics, Faculty of Electrical Engineering and Information Technology, Slovak University of Technology, 841 04 Bratislava, Slovakia., Tkac J; Institute of Chemistry, Slovak Academy of Sciences, 841 04 Bratislava, Slovakia. |
| Abstrakt: |
We investigated the use of boron-doped diamond (BDD) with different surface morphologies for the enhanced detection of nine different peptides by matrix-assisted laser desorption/ionisation mass spectrometry (MALDI-MS). For the first time, we compared three different nanostructured BDD film morphologies (Continuous, Nanograss, and Nanotips) with differently terminated surfaces (-H, -O, and -F) to commercially available Ground Steel plates. All these surfaces were evaluated for their effectiveness in detecting the nine different peptides by MALDI-MS. Our results demonstrated that certain nanostructured BDD surfaces exhibited superior performance for the detection of especially hydrophobic peptides (e.g., bradykinin 1-7, substance P, and the renin substrate), with a limit of detection of down to 2.3 pM. Further investigation showed that hydrophobic peptides (e.g., bradykinin 1-7, substance P, and the renin substrate) were effectively detected on hydrogen-terminated BDD surfaces. On the other hand, the highly acidic negatively charged peptide adrenocorticotropic hormone fragment 18-39 was effectively identified on oxygen-/fluorine-terminated BDD surfaces. Furthermore, BDD surfaces reduced sodium adduct contamination significantly. |
