How to make big molecules fly out of liquid water: applications, features and physics of laser assisted liquid phase dispersion mass spectrometry.
Applications, features, and mechanistic details of laser assisted liquid phase dispersion mass spectrometry are highlighted and discussed. It has been used in the past to directly isolate charged molecular aggregates from the liquid phase and to determine their molecular weight employing sensitive time-of-flight mass spectrometry. The liquid matrix in this MALDI (matrix assisted laser desorption and ionization) type approach consists of a 10 microm diameter free liquid filament in vacuum (or a free droplet) which is excited with a focused infrared laser pulse tuned to match the absorption frequency of the OH-stretch vibration of bulk water near 2.8 microm. Due to these features we will refer to the approach as free liquid matrix assisted laser dispersion of ions or ionic aggregates (IR-FL-MALDI), although also LILBID ("laser induced liquid beam (bead) desorption and ionization") has been proposed early as a descriptive acronym for the technique and may be used alternatively. Low-charge-state macromolecular adducts are isolated in the gas phase from solution via a yet poorly characterized mechanism which sensitively depends upon the laser intensity and wavelength, and after the gentle liquid-to-vacuum transfer the aggregates are analyzed via time-of-flight (TOF) mass spectrometry (MS). Possible mechanisms for the isolation and charging of biomolecules directly from liquid solution are discussed in the present contribution. Recent technical advances such as minimizing the sample consumption, strategies for high throughput mass spectrometry, and coupling of liquid beam MS with HPLC will be highlighted as well. An interesting feature of IR-FL-MALDI is what we call the linear response, i.e., a surprising linearity of the gas phase mass signal on the solution concentration over many orders of magnitude for a large number of biomolecular systems as well as ions. Due to these features the approach may be regarded as a true solution probing spectroscopy, which enables elegant biokinetic studies. Several experiments in which time resolved IR-FL-MALDI-MS has recently been employed successfully are given. A particular highlight is the possibility to quantitatively detect oxidation states in solution, which clearly distinguishes the present approach from other established MS source concepts. Due to the good matrix tolerance also proteins in complex mixtures can be monitored quantitatively.
Max-Planck Institut für biophysikalische Chemie, Am Fassberg 11, 37077, Göttingen, Germany.
Ales
A
Charvat
Bernd
B
Abel
D002851:Chromatography, High Pressure Liquid; D006454:Hemoglobins / Q000737:chemistry; D007259:Infrared Rays; D007477:Ions / Q000737:chemistry; D007700:Kinetics; D007834:Lasers; D046911:Macromolecular Substances / Q000737:chemistry*; D008954:Models, Biological; D044367:Phase Transition; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D014867:Water / Q000737:chemistry*
D006454:Hemoglobins; D007477:Ions; D046911:Macromolecular Substances; D011506:Proteins; D014867:Water