Detection of In Situ Derivatized Peptides in Microbial Biofilms by Laser Desorption 7.87 eV Postionizaton Mass Spectrometry
| Autor: | Carol S. Giometti, Michael J. Pellin, Kelly A. Skinner-Nemec, Jerry E. Hunt, J.F. Moore, Igor V. Veryovkin, Carl Lindberg, Luke Hanley, Praneeth D. Edirisinghe |
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| Rok vydání: | 2006 |
| Předmět: |
MALDI imaging
chemistry.chemical_classification Chromatography Protein mass spectrometry Quorum Sensing Peptide Mass spectrometry Analytical Chemistry Matrix-assisted laser desorption/ionization chemistry.chemical_compound chemistry Biofilms Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Desorption Amino Acid Sequence Peptides Derivatization Peptide sequence Bacillus subtilis |
| Zdroj: | Analytical Chemistry. 79:508-514 |
| ISSN: | 1520-6882 0003-2700 |
| DOI: | 10.1021/ac0615605 |
| Popis: | A novel analytical method based on laser desorption postionization mass spectrometry (LDPI-MS) was developed to investigate the competence and sporulation factor-a pentapeptide of amino acid sequence ERGMT-within intact Bacillus subtilis biofilms. Derivatization of the neat ERGMT peptide with quinoline- and anthracene-based tags was separately used to lower the peptide ionization potential and permit direct ionization by 7.87-eV vacuum ultraviolet radiation. The techniques of mass shifting and selective ionization of the derivatized peptide were combined here to permit detection of ERGMT peptide within intact biofilms by LDPI-MS, without any prior extraction or chromatographic separation. Finally, imaging MS specific to the derivatized peptide was demonstrated on an intact biofilm using LDPI-MS. The presence of ERGMT in the biofilms was verified by bulk extraction/LC-MS. However, MALDI imaging MS analyses were unable to detect ERGMT within intact biofilms. |
| Databáze: | OpenAIRE |
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