Desorption/Ionization Efficiency of Common Amino Acids in. Surface-assisted Laser Desorption/ionization Mass Spectrometry

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1 SUPPORTING INFORMATION Desorption/Ionization Efficiency of Common Amino Acids in Surface-assisted Laser Desorption/ionization Mass Spectrometry (SALDI-MS) with Nanostructured Platinum Syuhei Nitta, Hideya Kawasaki, Takashi Suganuma, Yasushi Shigeri, and Ryuichi Arakawa Department of Chemistry and Materials Engineering, Faculty of Chemistry, Materials and Bioengineering, Kansai University, Yamate-cho, Suita-shi, Osaka , Japan Health Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Midorigaoka, Ikeda, Osaka , Japan

2 (a) (b) (c) (d) (e) (f) Figure S. SEM images of Pt Nfs supported on silicon substrates prepared at different reaction temperatures: (a) 5 C, (b) 5 C, and (c) 5 C. [H PtCl 6 ] = mm, and the reaction time was h. The SEM images of Pt Nfs supported on silicon substrates prepared with different reaction concentrations of H PtCl 6 : (d) 0. mm, (e) mm, and (f) 0 mm. The reaction temperature was 5 C, and the reaction time was h. Scale bar = 300 nm. The higher temperature above 5 C enhanced the growth of Pt Nfs, while the higher concentration of H PtCl 6 at 0 mm suppressed the the growth of Pt Nfs.

3 (a) (b) (c) (d) (e) (f) (g) (h) Figure S. SEM images of Pt Nfs supported on silicon substrates prepared with different concentrations of HF: (a) 0. M, (b) M, (c) 5 M, and (d) 0 M. [H PtCl 6 ] = mm, and the reaction time was h. SEM images of Pt Nfs supported on silicon substrates prepared with different concentrations of HF: (e) 0. M, (f) M, (g) 5 M, and (h) 0 M. [H PtCl 6 ] = mm, and the reaction time was h. Scale bar = 300 nm. The higher concentration of HF above M enhanced the growth of Pt Nfs. 3

4 (a) Positive Sample peak :Unknown peak from Pt nanopartciles (b) Negative :Unknown peak from Pt nanopartciles Figure S3. SALDI mass spectra of the mixture of 0 amino acids using spherical Pt-nanoparticles in (a) positive and (b) negative ion modes.. [Pro+H] +,. [Ser+Na] +, 3. [Leu+H] +,. [Ile+H] +, 5. [Lys+H] +, 6. [Gln+H] +, 7. [Glu+H] +, 8. [His+H] +, 9. [Arg+H] +, 0. [Arg+Na] +. The two layer sample preparation method was employed for SALDI-MS of amino acids with Pt nanopartcles: the first step was spottingof the Pt nanoparticle-solution ( L, 5 mg/ml), prepared by dispersing Pt nanopartcles in pure water with ultrasonication for 5 min on a stainless steel plate, followed by drying; the second step was typically deposition of a 0.5 L sample solution on the plate.

5 (a) Positive ion 6 Sample peak Matrix peak (b) Negative ion Sample peak Matrix peak Figure S. MALDI mass spectra of the mixture of 0 amino acids using CHCA matrix in (a) positive and (b) negative ion modes. The peaks [M + H] + in positive ion mode and [M - H] - in negative ion mode of amino acids were obtained by the MALDI-MS. The amino acid are denoted by the number:. Gly,. Ala, 3. Asp,. Glu, 5. Lys, 6. Arg, 7.His, 8. Asn, 9. Gln, 0. Ser,. Thr,. Tyr, 3. Phe,. Trp, 5. Cys (dimer), 6. Met, 7. Val, 8. Leu, 9. Ile, and 0. Pro. 5

6 (a) Positive [Arg+H] + Y= [M+H] + [AngII+H] + 00 Arginine [AngII+H] + [Met+H] + Methionine [AngII+H] (b) Negative [Asp-H] - Y= [M H] [AngII H] Aspartic acid [AngII-H] - [Met-H] - Methionine [AngII-H] Figure S5. SALDI mass spectra using FDTS-Pt Nf chips of (a) Arg and Met in positive ion mode and (b) Asp and Met in negative ion mode. The ion yields (Y) were defined as the ratio of the peak intensity of the amino acid to that of Ang II. 6

7 (a) Positive [M+H] + 3, 35, 5: Not detected Detected (b) Negative [M-H] Figure S6. SALDI mass spectra using FDTS-Pt Nf chips of the mixture of five peptides:. Gly-Tyr-Ser-Arg-Arg,. Gly-Tyr-Ser-Ser-Arg, 3. Gly-Tyr-Ser-Asp-Asp,. Gly-Tyr-Ser-Ser-Asp, and 5. Gly-Tyr-Ser-Ser-Ser in (a) positive and (b) negative ion mode. 7

8 Table S. Relative intensity of [M+H] + and [M-H] - measured for free amino acids in positive ion and negative ion modes, values of proton affinity ), gas phase acidity ), B&B hydrophobicity ΔF 3), and monoisotopic mass (Mm) of amino acids. Amino acids Asp Glu Monoisotopic mass (Da) PA(kcal/mol) GA(kcal/mol) a b B&B hydrophobicity (kcal/mol) Relative Intensity [M+H] Relative Intensity [M-H] His Gln Asn Arg Ser Cys Thr Met Lys Phe Tyr Trp Ile Leu Val Pro Ala Gly c Detected as dimer, a Theoretical value from Ref., b Not determined, c Value taken from Ref.. REFERENCES ) Harrison, A. G. Mass Spectrom. Rev. 997, 6, 0. ) Colyer, K. E.; Jones, C. M.; Metz, R. A.; Pawlow, A. K.; Wischow, E. D.; Poutsma, J. C. Proceedings of the 5th ASMS Conference on Mass Spectrometry and Allied Topics, Seattle, 006, TP 5. 3) Bull, H. B.; Arch, B. K. Biochem. Biophys. 97, 6, 665. ) O Hair, R. A. J.; Bowie, J. H.; Gronert, S. Int. J. Mass Spectrom. 99, 7, 3. 8

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