journal article·2007-12-01

First Observation of Charge Reduction and Desorption Kinetics of Multiply Protonated Peptides Soft Landed onto Self-Assembled Monolayer Surfaces

Omar Hadjar, Jean H. Futrell, Julia Laskin

The Journal of Physical Chemistry C· Volume 111· Issue 49
Publisher page

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 ↗