Whole cell matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and in situ structure analysis of streptocidins, a family of tyrocidine-like cyclic peptides
Article first published online: 21 SEP 2005
Copyright © 2005 John Wiley & Sons, Ltd.
Rapid Communications in Mass Spectrometry
Volume 19, Issue 20, pages 2935–2942, 30 October 2005
How to Cite
Hitzeroth, G., Vater, J., Franke, P., Gebhardt, K. and Fiedler, H.-P. (2005), Whole cell matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and in situ structure analysis of streptocidins, a family of tyrocidine-like cyclic peptides. Rapid Commun. Mass Spectrom., 19: 2935–2942. doi: 10.1002/rcm.2155
- Issue published online: 21 SEP 2005
- Article first published online: 21 SEP 2005
- Manuscript Revised: 19 AUG 2005
- Manuscript Accepted: 19 AUG 2005
- Manuscript Received: 19 MAY 2005
- European Commission. Grant Number: QLK3-CT2001-01783-ACTAPHARM
Streptocidins, a family of tyrocidine-like cyclic decapeptides, are an ideal demonstration object for the detection and in situ structure analysis of natural compounds directly in microbial cells using whole cell matrix-assisted laser desorption/ionization time-of-flight-mass spectrometry (MALDI-TOFMS), an emerging technique that can be used for rapid sensitive metabolic profiling of microorganisms. Five main members of the streptocidin family (A–E) were detected in Brevibacillus cells picked from agar plates and identified by in situ structure analysis with post-source decay MALDI-TOFMS. This efficient modern method allows the precise detection of metabolites within minutes without the need to isolate and purify the target compounds. The generated mass spectra are of similar quality to those obtained for the purified peptides. In addition, surface extracts were prepared by treating Brevibacillus cells with 70% acetonitrile in the presence of 0.1% trifluoroacetic acid and fractionated by high-resolution reversed-phase high-performance liquid chromatography (HPLC). In this way ten minor streptocidins were detected demonstrating the full biosynthetic variety of streptocidin production on the cellular level. The streptocidins differ from the well-known tyrocidines essentially in position 3 of the decapeptide chain by replacement of the aromatic amino acid (F/W) found in tyrocidines by L-leucine or L-valine. Copyright © 2005 John Wiley & Sons, Ltd.