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Anal Chem. 1995 Nov 15;67(22):4139-44.

Attomole biomolecule mass analysis by matrix-assisted laser desorption/ionization Fourier transform ion cyclotron resonance.

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Center for Interdisciplinary Magnetic Resonance, National High Magnetic Field Laboratory, Florida State University, Tallahassee 32310, USA.


Significantly improved sensitivity for analysis of biomolecules by MALDI FT-ICR mass spectrometry is achieved by (i) microscope-monitored sample deposition onto a small indentation on the probe tip and (ii) multiple remeasurement of ions from a single laser shot. A simple modification to the solids probe tip allows for microdeposition of a few amols of analyte onto small indentation spots previously aligned with the laser beam. Ion multiple remeasurement of the same ion packet enhances the signal-to-noise ratio and thus extends the achievable FT-ICR MS detection limit. We demonstrate that FT-ICR can be used to detect parent and structurally significant fragment ions of peptides and phospholipids at low amol amounts. Positive ion mass spectra for approximately 90 amol of a mixture of angiotensin II and bradykinin, approximately 40 amol of dipalmitoylglycerophosphatidylcholine, and approximately 8 amol of substance P constitute the lowest reported detection limits to date for FT-ICR mass analysis of MALDI-generated ions.

[Indexed for MEDLINE]

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