First Observation of Charge Reduction and Desorption Kinetics of Multiply Protonated Peptides Soft Landed onto Self-Assembled Monolayer Surfaces
Source abstract
Abstract
The kinetics of charge reduction and desorption of different species produced by soft-landing of mass-selected ions was studied using in situ secondary ion mass spectrometry (SIMS) in a Fourier transform ion cyclotron resonance mass spectrometer (FT-ICR MS). The improved SIMS capability described in this work utilizes an in-line 8 keV Cs + ion gun and allows us to interrogate the surface both during the ion deposition and after the deposition is terminated. As a model system doubly protonated ions of Gramicidin S were deposited onto a fluorinated self-assembled monolayer (FSAM) surface. Our results demonstrate for the first time that various peptide-related peaks in FT-ICR SIMS spectra follow very different kinetics. We obtained unique kinetics signatures for doubly protonated, singly protonated and neutral peptides retained on the surface and followed their evolution as a function of time. The experimental results are in excellent agreement with a kinetic model that takes into account charge reduction and thermal desorption of different species from the surface.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Ion-surface interactions and analysis · Mass Spectrometry Techniques and Applications · Molecular Junctions and Nanostructures
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Pacific Northwest National Laboratory, Fundamental Science Directorate, Richland, Washington 99352
References (28)
Show source-provided references
1. Franchetti V. · Int. J. Mass Spectrom Ion Processes · 1977 · 23 · 2910.1016/0020-7381(77)80004-1 ↗
2. Miller S. A. · Science · 1997 · 275 · 144710.1126/science.275.5305.1447 ↗
3. Luo H. · Int. J. Mass Spectrom. · 1998 · 174 · 19310.1016/S0168-1176(97)00302-9 ↗
4. Denault J. W. · Anal. Chem. · 2000 · 72 · 579810.1021/ac0005823 ↗
5. Gologan B. · Phys. Chem. Chem. Phys. · 2005 · 7 · 149010.1039/b418056a ↗
6. Ouyang Z. · Science · 2003 · 301 · 135110.1126/science.1088776 ↗
7. Gologan B. · J. Am. Soc. Mass Spectrom. · 2004 · 15 · 187410.1016/j.jasms.2004.09.005 ↗
8. Volný M. · Anal. Chem. · 2005 · 77 · 484610.1021/ac0505019 ↗
9. Volny M. · Anal. Chem. · 2005 · 77 · 489010.1021/ac0507136 ↗
10. Kaiser B. · Phys. Rev. Lett. · 1999 · 83 · 291810.1103/PhysRevLett.83.2918 ↗
11. Palmer R. E. · Nat. Mater. · 2003 · 2 · 44310.1038/nmat897 ↗
12. Bottcher A. · Phys. Chem. Chem. Phys. · 2004 · 6 · 521310.1039/B413464H ↗
13. Bottcher A. · Phys. Chem. Chem. Phys. · 2005 · 7 · 281610.1039/b505703e ↗
14. Yamaguchi W. · Chem. Phys. Lett. · 1999 · 311 · 34110.1016/S0009-2614(99)00891-X ↗
15. Nagaoka S. · J. Am. Chem. Soc. · 2007 · 129 · 152810.1021/ja068442j ↗
16. Alvarez J. · J. Phys. Chem. A · 2006 · 110 · 167810.1021/jp0555044 ↗
17. Love J. C. · Chem. Rev. · 2005 · 105 · 110310.1021/cr0300789 ↗
18. Chechik V. · Adv. Mater. · 2000 · 12 · 116110.1002/1521-4095(200008)12:16<1161::AID-ADMA1161>3.0.CO;2-C ↗
19. Dongre A. R. · J. Mass Spectrom. · 1996 · 31 · 33910.1002/(SICI)1096-9888(199604)31:4<339::AID-JMS322>3.0.CO;2-L ↗
20. Grill V. · Rev. Sci. Instrum. · 2001 · 72 · 314910.1063/1.1382641 ↗
21. Gologan B. · 2006
22. Laskin J. · J. Am. Soc. Mass Spectrom. · 2003 · 14 · 134010.1016/j.jasms.2003.08.004 ↗
23. Alvarez J. · Anal. Chem. · 2005 · 77 · 345210.1021/ac0481349 ↗
24. Laskin J. · Int. J. Mass Spectrom. · 2007 · 265 · 23710.1016/j.ijms.2007.02.013 ↗
25. Laskin J. · Anal. Chem. · 2002 · 74 · 325510.1021/ac025514q ↗
26. Hadjar O. · Anal. Chem. · 2007 · 79 · 656710.1021/ac070600h ↗
27. Senko M. W. · Rapid Comm. Mass Spectrom. · 1996 · 10 · 183910.1002/(SICI)1097-0231(199611)10:14<1839::AID-RCM718>3.0.CO;2-V ↗
28. Chidsey C. · J. Chem. Phys. · 1989 · 91 · 442110.1063/1.456776 ↗