A study of peptide-peptide interactions using MALDI ion mobility o-TOF and ESI mass spectrometry.
Matrix-assisted laser desorption ionization ion mobility coupled to orthogonal time-of-flight mass spectrometry (MALDI-IM-oTOF MS) is evaluated as a tool for studying non-covalent complex (NCX) formation between peptides. The NCX formed between dynorphin 1-7 and Mini Gastrin I is used as a model system for comparison to previous MALDI experiments (Woods, A. S.; Huestis, M. A. J. Am. Soc. Mass Spectrom. 2001, 12, 88-96). The dynorphin 1-7/Mini Gastrin I complex is stable after more than a ms drift time through the He filled mobility cell. Furthermore, the effects of solution pH on NCX ion signal intensity is measured both by MALDI-IM-MS analysis and by nanoelectrospray mass spectrometry. When compared to the previous MALDI study this work shows that all three techniques give similar results. In addition, fragmentation can be observed from of the non-covalent complex parent ion that occurs prior to TOF mass analysis but after mobility separation, thus providing NCX composition information.
Woods
Amina S
AS
Chemistry and Drug Metabolism, Intramural Research Program, NIDA, NIH, Baltimore, MD 21224, USA. awoods@intra.nida.nih.gov
Koomen
John M
JM
Ruotolo
Brandon T
BT
Gillig
Kent J
KJ
Russel
David H
DH
Fuhrer
Katrin
K
Gonin
Marc
M
Egan
Thomas F
TF
Schultz
J Albert
JA
D017869:Cyclic GMP-Dependent Protein Kinases / Q000378:metabolism; D004399:Dynorphins / Q000737:chemistry; D005755:Gastrins / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D010455:Peptides / Q000737:chemistry*; D021241:Spectrometry, Mass, Electrospray Ionization; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D005755:Gastrins; D010455:Peptides; C061479:protein kinase inhibitor peptide; C008530:minigastrin; D004399:Dynorphins; D017869:Cyclic GMP-Dependent Protein Kinases