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Journal articles on the topic 'MALDI-MS/MS'

Author: Grafiati

Published: 6 September 2023

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1

Chin, Jefferson, Elizabeth Wood, Grace S. Peters, and Dieter M. Drexler. "Acoustic Sample Deposition MALDI-MS (ASD-MALDI-MS)." Journal of Laboratory Automation 21, no. 1 (February 2016): 204–7. http://dx.doi.org/10.1177/2211068215594769.

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2

NIRASAWA, TAKASHI. "MALDI-TOF-MS." Kagaku To Seibutsu 34, no. 4 (1996): 255–59. http://dx.doi.org/10.1271/kagakutoseibutsu1962.34.255.

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3

Darie-Ion, Laura, Danielle Whitham, Madhuri Jayathirtha, Yashveen Rai, Anca-Narcisa Neagu, Costel C. Darie, and Brînduşa Alina Petre. "Applications of MALDI-MS/MS-Based Proteomics in Biomedical Research." Molecules 27, no. 19 (September 21, 2022): 6196. http://dx.doi.org/10.3390/molecules27196196.

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Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) is one of the most widely used techniques in proteomics to achieve structural identification and characterization of proteins and peptides, including their variety of proteoforms due to post-translational modifications (PTMs) or protein–protein interactions (PPIs). MALDI-MS and MALDI tandem mass spectrometry (MS/MS) have been developed as analytical techniques to study small and large molecules, offering picomole to femtomole sensitivity and enabling the direct analysis of biological samples, such as biofluids, solid tissues, tissue/cell homogenates, and cell culture lysates, with a minimized procedure of sample preparation. In the last decades, structural identification of peptides and proteins achieved by MALDI-MS/MS helped researchers and clinicians to decipher molecular function, biological process, cellular component, and related pathways of the gene products as well as their involvement in pathogenesis of diseases. In this review, we highlight the applications of MALDI ionization source and tandem approaches for MS for analyzing biomedical relevant peptides and proteins. Furthermore, one of the most relevant applications of MALDI-MS/MS is to provide “molecular pictures”, which offer in situ information about molecular weight proteins without labeling of potential targets. Histology-directed MALDI-mass spectrometry imaging (MSI) uses MALDI-ToF/ToF or other MALDI tandem mass spectrometers for accurate sequence analysis of peptide biomarkers and biological active compounds directly in tissues, to assure complementary and essential spatial data compared with those obtained by LC-ESI-MS/MS technique.

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4

Pashkova, Anna, Eugene Moskovets, and Barry L. Karger. "Coumarin Tags for Improved Analysis of Peptides by MALDI-TOF MS and MS/MS. 1. Enhancement in MALDI MS Signal Intensities." Analytical Chemistry 76, no. 15 (August 2004): 4550–57. http://dx.doi.org/10.1021/ac049638+.

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5

Yang, Hyo-Jik, Kyu Hwan Park, Seongjae Shin, Ji-hye Lee, Sehwan Park, Hyun Sik Kim, and Jeongkwon Kim. "Characterization of heme ions using MALDI-TOF MS and MALDI FT-ICR MS." International Journal of Mass Spectrometry 343-344 (June 2013): 37–44. http://dx.doi.org/10.1016/j.ijms.2013.03.014.

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6

Rappsilber, Juri, Marc Moniatte, Michael L. Nielsen, Alexandre V. Podtelejnikov, and Matthias Mann. "Experiences and perspectives of MALDI MS and MS/MS in proteomic research." International Journal of Mass Spectrometry 226, no. 1 (March 2003): 223–37. http://dx.doi.org/10.1016/s1387-3806(02)00976-4.

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7

Zhang, Nan, Nan Li, and Liang Li. "Liquid Chromatography MALDI MS/MS for Membrane Proteome Analysis." Journal of Proteome Research 3, no. 4 (August 2004): 719–27. http://dx.doi.org/10.1021/pr034116g.

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8

Schiller, Jurgen. "MALDI-TOF MS in lipidomics." Frontiers in Bioscience 12, no. 1 (2007): 2568. http://dx.doi.org/10.2741/2255.

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9

Haff, L., P. Juhasz, S. Martin, M. Roskey, I. Smirnov, W. Stanick, M. Vestal, and K. Waddell. "Oligonucleotide analysis by MALDI-MS." Analusis 26, no. 10 (December 1998): 26–30. http://dx.doi.org/10.1051/analusis:1998260026.

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10

Schuerenberg, Martin, Christine Luebbert, Holger Eickhoff, Markus Kalkum, Hans Lehrach, and Eckhard Nordhoff. "Prestructured MALDI-MS Sample Supports." Analytical Chemistry 72, no. 15 (August 2000): 3436–42. http://dx.doi.org/10.1021/ac000092a.

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11

Paulus, Gerd, and Martin Resch. "Molmassen-Bestimmung mittels MALDI-MS." Nachrichten aus Chemie, Technik und Laboratorium 42, no. 7-8 (July 1994): 719–22. http://dx.doi.org/10.1002/nadc.19940420713.

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12

Sousa, Roberto B., Keila S. C. Lima, Caleb G. M. Santos, Tanos C. C. França, Eugenie Nepovimova, Kamil Kuca, Marcos R. Dornelas, and Antonio L. S. Lima. "A New Method for Extraction and Analysis of Ricin Samples through MALDI-TOF-MS/MS." Toxins 11, no. 4 (April 3, 2019): 201. http://dx.doi.org/10.3390/toxins11040201.

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We report for the first time the efficient use of accelerated solvent extraction (ASE) for extraction of ricin to analytical purposes, followed by the combined use of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), and MALDI-TOF MS/MS method. That has provided a fast and unambiguous method of ricin identification for in real cases of forensic investigation of suspected samples. Additionally, MALDI-TOF MS was applied to characterize the presence and the toxic activity of ricin in irradiated samples. Samples containing ricin were subjected to ASE, irradiated with different dosages of gamma radiation, and analyzed by MALDI-TOF MS/MS for verification of the intact protein signal. For identification purposes, samples were previously subjected to SDS-PAGE, for purification and separation of the chains, followed by digestion with trypsin, and analysis by MALDI-TOF MS/MS. The results were confirmed by verification of the amino acid sequences of some selected peptides by MALDI-TOF MS/MS. The samples residual toxic activity was evaluated through incubation with a DNA substrate, to simulate the attack by ricin, followed by MALDI-TOF MS/MS analyses.

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13

Rim, John Hoon, Yangsoon Lee, Sung Kuk Hong, Yongjung Park, MyungSook Kim, Roshan D’Souza, Eun Suk Park, Dongeun Yong, and Kyungwon Lee. "Insufficient Discriminatory Power of Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry Dendrograms to Determine the Clonality of Multi-Drug-ResistantAcinetobacter baumanniiIsolates from an Intensive Care Unit." BioMed Research International 2015 (2015): 1–8. http://dx.doi.org/10.1155/2015/535027.

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While pulsed-field gel electrophoresis (PFGE) is recognized as the gold standard method for clonality analysis, MALDI-TOF MS has recently been spotlighted as an alternative tool for species identification. Herein, we compared the dendrograms of multi-drug-resistant (MDR)Acinetobacter baumanniiisolates by using MALDI-TOF MS with those by using PFGE. We used direct colony and protein extraction methods for MALDI-TOF MS dendrograms. The isolates with identical PFGE patterns were grouped into different branches in MALDI-TOF MS dendrograms. Among the isolates that were classified as very close isolates in MALDI-TOF MS dendrogram, PFGE band patterns visually showed complete differences. We numeralized similarity among isolates by measuring distance levels. The Spearman rank correlation coefficient values were 0.449 and 0.297 between MALDI-TOF MS dendrogram using direct colony and protein extraction method versus PFGE, respectively. This study is the first paper focusing solely on the dendrogram function of MALDI-TOF MS compared with PFGE. Although MALDI-TOF MS is a promising tool to identify species in a rapid manner, our results showed that MALDI-TOF MS dendrograms could not substitute PFGE for MDRAcinetobacter baumanniiclonality analysis.

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14

Dell, Anne, Howard R. Morris, Richard Easton, Stuart Haslam, Maria Panico, Mark Sutton-Smith, Andrew J. Reason, and Kay-Hooi Khoo. "ChemInform Abstract: Structural Analysis of Oligosaccharides: FAB-MS, ES-MS and MALDI-MS." ChemInform 32, no. 11 (March 13, 2001): no. http://dx.doi.org/10.1002/chin.200111299.

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15

Chen, Xin-Fei, Xin Hou, Meng Xiao, Li Zhang, Jing-Wei Cheng, Meng-Lan Zhou, Jing-Jing Huang, Jing-Jia Zhang, Ying-Chun Xu, and Po-Ren Hsueh. "Matrix-Assisted Laser Desorption/Ionization Time of Flight Mass Spectrometry (MALDI-TOF MS) Analysis for the Identification of Pathogenic Microorganisms: A Review." Microorganisms 9, no. 7 (July 19, 2021): 1536. http://dx.doi.org/10.3390/microorganisms9071536.

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Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) has been used in the field of clinical microbiology since 2010. Compared with the traditional technique of biochemical identification, MALDI-TOF MS has many advantages, including convenience, speed, accuracy, and low cost. The accuracy and speed of identification using MALDI-TOF MS have been increasing with the development of sample preparation, database enrichment, and algorithm optimization. MALDI-TOF MS has shown promising results in identifying cultured colonies and rapidly detecting samples. MALDI-TOF MS has critical research applications for the rapid detection of highly virulent and drug-resistant pathogens. Here we present a scientific review that evaluates the performance of MALDI-TOF MS in identifying clinical pathogenic microorganisms. MALDI-TOF MS is a promising tool in identifying clinical microorganisms, although some aspects still require improvement.

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16

Sun, Ai-dong. "Isolation and Identification of procyanidins in Aronia Melanocarpa Using NMR, LC-IT-TOF/MS/MS and MALDI-TOF MS." SDRP Journal of Food Science & Technology 4, no. 2 (2019): 614–28. http://dx.doi.org/10.25177/jfst.4.1.ra.444.

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17

Kaleta, Erin J., Andrew E. Clark, Abdessalam Cherkaoui, Vicki H. Wysocki, Elizabeth L. Ingram, Jacques Schrenzel, and Donna M. Wolk. "Comparative Analysis of PCR–Electrospray Ionization/Mass Spectrometry (MS) and MALDI-TOF/MS for the Identification of Bacteria and Yeast from Positive Blood Culture Bottles." Clinical Chemistry 57, no. 7 (July 1, 2011): 1057–67. http://dx.doi.org/10.1373/clinchem.2011.161968.

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BACKGROUND Emerging technologies for rapid identification of microbes demonstrate a shift from traditional biochemical and molecular testing algorithms toward methods using mass spectrometry (MS) for the semiquantitative analysis of microbial proteins and genetic elements. This study was performed to assess the diagnostic accuracy of 2 such technologies, PCR–electrospray ionization (ESI)/MS and MALDI-TOF/MS, with respect to phenotypic and biochemical profiling as a reference standard method. A positive challenge set of blood culture bottles was used to compare PCR-ESI/MS and MALDI-TOF/MS performance on a matched set of samples. METHODS We performed characterization of bloodstream infections from blood cultures using the Ibis T5000 PCR-ESI/MS and the Bruker MALDI Biotyper 2.0 (MALDI-TOF/MS) platforms for microbial identification. Diagnostic accuracy was determined by independent comparison of each method to phenotypic and biochemical characterization with Vitek2 analysis as the reference standard identification. RESULTS The diagnostic accuracy, represented as positive agreement, at the genus level was 0.965 (0.930–0.984) for PCR-ESI/MS and 0.969 (0.935–0.987) for MALDI-TOF/MS, and at the species level was 0.952 (0.912–0.974) with PCR-ESI/MS and 0.943 (0.902–0.968) for MALDI-TOF/MS. No statistically significant difference was found between PCR-ESI/MS and MALDI-TOF/MS in the ability to rapidly identify microorganisms isolated from blood culture. CONCLUSIONS Our results demonstrate that PCR-ESI/MS and MALDI-TOF/MS are equivalent in their ability to characterize bloodstream infections with respect to the reference standard, and highlight key differences in the methods that allow for each method to have a unique niche as a tool for rapid identification of microbes in blood cultures.

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18

Potier, N., V. Lamour, A. Poterszman, J. C. Thierry, D. Moras, and A. Van Dorsselaer. "Characterization of crystal content by ESI–MS and MALDI–MS." Acta Crystallographica Section D Biological Crystallography 56, no. 12 (December 1, 2000): 1583–90. http://dx.doi.org/10.1107/s0907444900010271.

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19

Hercules, David M. "Polymer MS-MS by MALDI: some advances and some challenges." Analytical and Bioanalytical Chemistry 392, no. 4 (August 4, 2008): 571–73. http://dx.doi.org/10.1007/s00216-008-2298-z.

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20

Israr, Muhammad Zubair, Dennis Bernieh, Andrea Salzano, Shabana Cassambai, Yoshiyuki Yazaki, and Toru Suzuki. "Matrix-assisted laser desorption ionisation (MALDI) mass spectrometry (MS): basics and clinical applications." Clinical Chemistry and Laboratory Medicine (CCLM) 58, no. 6 (June 25, 2020): 883–96. http://dx.doi.org/10.1515/cclm-2019-0868.

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AbstractBackgroundMatrix-assisted laser desorption ionisation (MALDI) mass spectrometry (MS) has been used for more than 30 years. Compared with other analytical techniques, it offers ease of use, high throughput, robustness, cost-effectiveness, rapid analysis and sensitivity. As advantages, current clinical techniques (e.g. immunoassays) are unable to directly measure the biomarker; rather, they measure secondary signals. MALDI-MS has been extensively researched for clinical applications, and it is set for a breakthrough as a routine tool for clinical diagnostics.ContentThis review reports on the principles of MALDI-MS and discusses current clinical applications and the future clinical prospects for MALDI-MS. Furthermore, the review assesses the limitations currently experienced in clinical assays, the advantages and the impact of MALDI-MS to transform clinical laboratories.SummaryMALDI-MS is widely used in clinical microbiology for the screening of microbial isolates; however, there is scope to apply MALDI-MS in the diagnosis, prognosis, therapeutic drug monitoring and biopsy imaging in many diseases.OutlookThere is considerable potential for MALDI-MS in clinic as a tool for screening, profiling and imaging because of its high sensitivity and specificity over alternative techniques.

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21

Beeman, Katrin, Jens Baumgärtner, Manuel Laubenheimer, Karlheinz Hergesell, Martin Hoffmann, Ulrich Pehl, Frank Fischer, and Jan-Carsten Pieck. "Integration of an In Situ MALDI-Based High-Throughput Screening Process: A Case Study with Receptor Tyrosine Kinase c-MET." SLAS DISCOVERY: Advancing the Science of Drug Discovery 22, no. 10 (August 18, 2017): 1203–10. http://dx.doi.org/10.1177/2472555217727701.

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Mass spectrometry (MS) is known for its label-free detection of substrates and products from a variety of enzyme reactions. Recent hardware improvements have increased interest in the use of matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) MS for high-throughput drug discovery. Despite interest in this technology, several challenges remain and must be overcome before MALDI-MS can be integrated as an automated “in-line reader” for high-throughput drug discovery. Two such hurdles include in situ sample processing and deposition, as well as integration of MALDI-MS for enzymatic screening assays that usually contain high levels of MS-incompatible components. Here we adapt our c-MET kinase assay to optimize for MALDI-MS compatibility and test its feasibility for compound screening. The pros and cons of the Echo (Labcyte) as a transfer system for in situ MALDI-MS sample preparation are discussed. We demonstrate that this method generates robust data in a 1536-grid format. We use the MALDI-MS to directly measure the ratio of c-MET substrate and phosphorylated product to acquire IC50 curves and demonstrate that the pharmacology is unaffected. The resulting IC50 values correlate well between the common label-based capillary electrophoresis and the label-free MALDI-MS detection method. We predict that label-free MALDI-MS-based high-throughput screening will become increasingly important and more widely used for drug discovery.

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22

Sharma, Ram Jee, Ramesh C. Gupta, Arvind Kumar Bansal, and Inder Pal Singh. "Metabolite Fingerprinting of Eugenia jambolana Fruit Pulp Extracts using NMR, HPLC-PDA-MS, GC-MS, MALDI-TOF-MS and ESI-MS/MS Spectrometry." Natural Product Communications 10, no. 6 (June 2015): 1934578X1501000. http://dx.doi.org/10.1177/1934578x1501000644.

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Eugenia jambolana, commonly known as ‘jamun’ or Indian blackberry, is an important source of bioactive compounds. All parts of the plant like stem bark, leaves, flower, fruit pulp and seeds are traditionally used for many diseases. Metabolite profiling in medicinally important plants is critical to resolve the problems associated with standardization and quality control. Metabolite profiling of the fruit pulp of Jamun was performed by NMR, HPLC, MS, GC-MS and MALDI-TOF mass spectrometry. These hyphenated techniques helped in the identification of 68 chemically-diverse metabolites of the fruit pulp. These include anthocyanins, anthocyanidins, sugars, phenolics and volatile compounds. Five extracts of fruit pulp were prepared i.e. hexane, chloroform, ethylacetate, butanol and aqueous methanolic. Twenty-five metabolites identified and quantified in the n-butanol and aqueous-methanolic extracts of ripe jamun fruit by qNMR. LC-PDA-MS and MALDI-TOF spectrometry helped in deciphering thirty-nine metabolites out of which thirteen were quantified.

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23

Madhavan, Anitha, Arun Sachu, Nandini Sethuraman, Anil Kumar, and Jayalakshmi Vasudevapanicker. "Evaluation of Matrix-assisted laser desorption/ionization Time-of flight Mass spectrometry (MALDI TOF MS) and VITEK 2 in routine microbial identification." Ghana Medical Journal 55, no. 4 (December 1, 2021): 308–10. http://dx.doi.org/10.4314/gmj.v55i4.12.

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Background: Microbial Identification was done by phenotypic methods. VITEK-2 and Matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) are now being increasingly used in laboratories.Objectives: To compare and evaluate the usefulness of MALDI-TOF MS and VITEK-2 in routine microbial identification.Methods: The performances of MALDI-TOF MS and VITEK 2 were compared for identifying microorganisms.Results: MALDI- TOF MS and VITEK-2 correctly identified 96 % (96/100) and 97% (97/100) of the isolates upto the genus level.Conclusion: MALDI TOF MS and VITEK -2 gave comparable identification and error rates. The rapid reduction in turnaround time with MALDI TOF is a significant game-changer in the field of clinical microbiology

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24

Kett, Warren C., and Deirdre R. Coombe. "A structural analysis of heparin‒like glycosaminoglycans using MALDI‒TOF mass spectrometry." Spectroscopy 18, no. 2 (2004): 185–201. http://dx.doi.org/10.1155/2004/392536.

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Mass spectrometry (MS) techniques have spear‒headed the field of proteomics. Recently, MS has been used to structurally analyse carbohydrates. The heparin/heparan sulfate‒like glycosaminoglycans (HLGAGs) present a special set of difficulties for structural analysis because they are highly sulfated and heterogeneous. We have used a matrix‒assisted laser desorption/ionization time of flight mass spectrometry (MALDI‒MS) technique in which heparin fragments are non‒covalently bound to basic peptides of a known mass, so as to limit in‒source desulfation and hence afford an accurate mass. We examined a range of different sized fragments with varying degrees of sulfation. The potential of combining the MALDI‒MS technique with enzymatic digestion to obtain saccharide sequence information on heparin fragments was explored. A disaccharide analysis greatly assists in determining a sequence from MALDI‒MS data. Enzymatic digestion followed by MALDI‒MS allows structural data on heparin fragments too large for direct MALDI‒MS to be obtained. We demonstrate that synthetic sulfated oligosaccharides can also be analysed by MALDI‒MS. There are advantages and limitations with this methodology, but until superior MS techniques become readily accessible to biomedical scientists the MALDI‒MS method provides a means to structurally analyse HLGAG fragments that have therapeutic potential because of their ability to bind to and functionally regulate a host of clinically important proteins.

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FUKUYAMA, Yuko. "MALDI MS Analysis Using Liquid Matrices." Journal of the Mass Spectrometry Society of Japan 64, no. 5 (2016): 175–78. http://dx.doi.org/10.5702/massspec.s16-36.

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26

Tan, Zhi Lei, Yu Qiao Wei, Shuang Liang, Ran Zhang, Miao Liu, and Shi Ru Jia. "Rapid Identification of Microorganisms Isolated from Pickled Vegetables by MALDI-TOF Mass Spectrometry." Advanced Materials Research 712-715 (June 2013): 494–97. http://dx.doi.org/10.4028/www.scientific.net/amr.712-715.494.

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Matrix-assisted laser desorption/ionization time-off light mass spectrometry (MALDI-TOF MS) is increasingly used as a microbial diagnostic method for species identification of pathogens. However, MALDI-TOF MS identification of food bacteria was seldom reported. Ten strains isolated from different pickled vegetables were rapid identified by MALDI-TOF MS. The results of MALDI-TOF MS were confirmed by 16S rDNA sequencing method. Different score values in MALDI-TOF MS revealed nineLeuconostoc mesenteroides and oneStaphylococcus.Identification success at the species and genus levels was 90% (9/10) and 100% (10/10), respectively.16S rDNA sequencing results showed that nine stains were identified asLeuconostoc mesenteroides and one wasStaphylococcus saprophyticus.Results obtained demonstrate that MALDI-TOFMS is a promising method for discriminating and identifying food bacteria.

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Chiappetta, Giovanni, Sega NDiaye, Emmanuelle Demey, Iman Haddad, Gennaro Marino, Angela Amoresano, and Joëlle Vinh. "Dansyl-peptides matrix-assisted laser desorption/ionization mass spectrometric (MALDI-MS) and tandem mass spectrometric (MS/MS) features improve the liquid chromatography/MALDI-MS/MS analysis of the proteome." Rapid Communications in Mass Spectrometry 24, no. 20 (September 22, 2010): 3021–32. http://dx.doi.org/10.1002/rcm.4734.

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Mareković, Ivana, Zrinka Bošnjak, Marko Jakopović, Zagorka Boras, Mateja Janković, and Sanja Popović-Grle. "Evaluation of Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry in Identification of Nontuberculous Mycobacteria." Chemotherapy 61, no. 4 (2016): 167–70. http://dx.doi.org/10.1159/000442517.

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Background/Aims: Species-level identification of nontuberculous mycobacteria (NTM) is important in making decisions about the necessity and choice of antimicrobial treatment. The reason is predictable clinical significance and the susceptibility profile of specific NTM species. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) is recognized as a diagnostic tool for routine identification of bacteria and yeasts in the clinical laboratory based on protein fingerprint analysis. The aim of the study was to evaluate MALDI-TOF MS in the identification of NTM. Methods: A total of 25 NTM isolates from liquid cultures were identified with both polymerase chain reaction (PCR)-based hybridization assay and MALDI-TOF MS at the University Hospital Center Zagreb. Results: PCR-based hybridization assay identified 96% (24/25) and MALDI-TOF MS 80% (20/25) of tested NTM isolates. Five isolates with no reliable MALDI-TOF MS identification belonged to the Mycobacterium avium-intracellulare complex. Seventy percent (14/20) of NTM isolates successfully identified with MALDI-TOF MS had a score higher than 2.0, indicating reliable species identification. Conclusion: MALDI-TOF MS is a promising tool for the identification of NTM. With a further improvement of the protein extraction protocol, especially regarding the M. avium-intracellulare complex, MALDI-TOF MS could be an additional standard method for identification of NTM.

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Han, Sang-Soo, Young-Su Jeong, and Sun-Kyung Choi. "Current Scenario and Challenges in the Direct Identification of Microorganisms Using MALDI TOF MS." Microorganisms 9, no. 9 (September 9, 2021): 1917. http://dx.doi.org/10.3390/microorganisms9091917.

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MALDI TOF MS-based microbial identification significantly lowers the operational costs because of minimal requirements of substrates and reagents for extraction. Therefore, it has been widely used in varied applications such as clinical, food, military, and ecological research. However, the MALDI TOF MS method is laced with many challenges including its limitation of the reference spectrum. This review briefly introduces the background of MALDI TOF MS technology, including sample preparation and workflow. We have primarily discussed the application of MALDI TOF MS in the identification of microorganisms. Furthermore, we have discussed the current trends for bioaerosol detection using MALDI TOF MS and the limitations and challenges involved, and finally the approaches to overcome these challenges.

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Oliveira, Thais Cristina de Assis, Maria Aparecida Vasconcelos Paiva Brito, Marcia Giambiagi-de Marval, Nívea Maria Vicentini, and Carla Christine Lange. "Identification of bovine mastitis pathogens using MALDI-TOF mass spectrometry in Brazil." Journal of Dairy Research 88, no. 3 (August 2021): 302–6. http://dx.doi.org/10.1017/s0022029921000595.

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AbstractIn this Research Communication we evaluate the use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) to identify 380 bacteria isolated from cases of bovine mastitis in Brazil. MALDI-TOF MS identifications were compared to previous identifications by biochemical tests and 16S rRNA sequencing. MALDI-TOF MS achieved a typeability of 95.5%. The accuracy of MALDI-TOF MS for the identification of Staphylococcus isolates was 93.2%. The agreement between MALDI-TOF MS and biochemical identification of Streptococcus agalactiae was 96%, however, the agreement between these techniques for identifying other catalase-negative, Gram-positive cocci was lower. Agreement in identifying Gram-negative bacteria at the genus level was 90.5%. Our findings corroborate that MALDI-TOF MS is an accurate, rapid and simple technique for identifying bovine mastitis pathogens. The availability of this methodology in some research institutions would represent a significant step toward increasing the diagnosis and epidemiological studies of bovine mastitis and other animal infectious diseases in Brazil.

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Chui, Huixia, Michael Chan, Drexler Hernandez, Patrick Chong, Stuart McCorrister, Alyssia Robinson, Matthew Walker, et al. "Rapid, Sensitive, and Specific Escherichia coli H Antigen Typing by Matrix-Assisted Laser Desorption Ionization–Time of Flight-Based Peptide Mass Fingerprinting." Journal of Clinical Microbiology 53, no. 8 (May 27, 2015): 2480–85. http://dx.doi.org/10.1128/jcm.00593-15.

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Matrix-assisted laser desorption ionization–time of flight mass spectrometry (MALDI-TOF MS) has gained popularity in recent years for rapid bacterial identification, mostly at the genus or species level. In this study, a rapid method to identify the Escherichia coli flagellar antigen (H antigen) at the subspecies level was developed using a MALDI-TOF MS platform with high specificity and sensitivity. Flagella were trapped on a filter membrane, and on-filter trypsin digestion was performed. The tryptic digests of each flagellin then were collected and analyzed by MALDI-TOF MS through peptide mass fingerprinting. Sixty-one reference strains containing all 53 H types and 85 clinical strains were tested and compared to serotyping designations. Whole-genome sequencing was used to resolve conflicting results between the two methods. It was found that DHB (2,5-dihydroxybenzoic acid) worked better than CHCA (α-cyano-4-hydroxycinnamic acid) as the matrix for MALDI-TOF MS, with higher confidence during protein identification. After method optimization, reference strains representing all 53 E. coli H types were identified correctly by MALDI-TOF MS. A custom E. coli flagellar/H antigen database was crucial for clearly identifying the E. coli H antigens. Of 85 clinical isolates tested by MALDI-TOF MS-H, 75 identified MS-H types (88.2%) matched results obtained from traditional serotyping. Among 10 isolates where the results of MALDI-TOF MS-H and serotyping did not agree, 60% of H types characterized by whole-genome sequencing agreed with those identified by MALDI-TOF MS-H, compared to only 20% by serotyping. This MALDI-TOF MS-H platform can be used for rapid and cost-effective E. coli H antigen identification, especially during E. coli outbreaks.

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Woods, Katherine, David Beighton, and John L. Klein. "Identification of the ‘Streptococcus anginosus group’ by matrix-assisted laser desorption ionization – time-of-flight mass spectrometry." Journal of Medical Microbiology 63, no. 9 (September 1, 2014): 1143–47. http://dx.doi.org/10.1099/jmm.0.076653-0.

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Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) provides rapid, accurate and cost-effective identification of a range of bacteria and is rapidly changing the face of routine diagnostic microbiology. However, certain groups of bacteria, for example streptococci (in particular viridans or non-haemolytic streptococci), are less reliably identified by this method. We studied the performance of MALDI-TOF MS for identification of the ‘Streptococcus anginosus group’ (SAG) to species level. In total, 116 stored bacteraemia isolates identified by conventional methods as belonging to the SAG were analysed by MALDI-TOF MS. Partial 16S rRNA gene sequencing, supplemented with sialidase activity testing, was performed on all isolates to provide ‘gold standard’ identification against which to compare MALDI-TOF MS performance. Overall, 100 % of isolates were correctly identified to the genus level and 93.1 % to the species level by MALDI-TOF MS. However, only 77.6 % were correctly identified to the genus level and 59.5 % to the species level by a MALDI-TOF MS direct transfer method alone. Use of a rapid in situ extraction method significantly improved identification rates when compared with the direct transfer method (P<0.001). We recommend routine use of this method to reduce the number of time-consuming full extractions required for identification of this group of bacteria by MALDI-TOF MS in the routine diagnostic laboratory. Only 22 % (1/9) of Streptococcus intermedius isolates were reliably identified by MALDI-TOF MS to the species level, even after full extraction. MALDI-TOF MS reliably identifies S. anginosus and Streptococcus constellatus to the species level but does not reliably identify S. intermedius.

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Osa, Morichika, Maria Cecilia Belo, Zita Dela Merced, Annavi Marie G. Villanueva, Jaira Mauhay, Alyannah Celis, Melissa Catli, et al. "Performance of MALDI–TOF Mass Spectrometry in the Philippines." Tropical Medicine and Infectious Disease 6, no. 3 (June 26, 2021): 112. http://dx.doi.org/10.3390/tropicalmed6030112.

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Identification of the causative pathogen in infectious diseases is important for surveillance and to guide treatment. In low- and middle-income countries (LMIC), conventional culture and identification methods, including biochemical methods, are reference-standard. Biochemical methods can lack sensitivity and specificity and have slow turnaround times, causing delays in definitive therapy. Matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI–TOF MS) is a rapid and accurate diagnostic method. Most studies comparing MALDI–TOF MS and biochemical methods are from high-income countries, with few reports from LMIC with tropical climates. The aim of this study was to assess the performance of MALDI–TOF MS compared to conventional methods in the Philippines. Clinical bacterial or fungal isolates were identified by both MALDI–TOF MS and automated (VITEK2) or manual biochemical methods in the San Lazaro Hospital, Metro Manila, the Philippines. The concordance between MALDI–TOF MS and automated (VITEK2) or manual biochemical methods was analyzed at the species and genus levels. In total, 3530 bacterial or fungal isolates were analyzed. The concordance rate between MALDI–TOF MS and biochemical methods was 96.2% at the species level and 99.9% at the genus level. Twenty-three isolates could not be identified by MALDI–TOF MS. In this setting, MALDI–TOF MS was accurate compared with biochemical methods, at both the genus and the species level. Additionally, MALDI–TOF MS improved the turnaround time for results. These advantages could lead to improved infection management and infection control in low- and middle-income countries, even though the initial cost is high.

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Bodnar, Wanda M., R. Kevin Blackburn, Jo M. Krise, and M. Arthur Moseley. "Exploiting the complementary nature of LC/MALDI/MS/MS and LC/ESI/MS/MS for increased proteome coverage." Journal of the American Society for Mass Spectrometry 14, no. 9 (September 2003): 971–79. http://dx.doi.org/10.1016/s1044-0305(03)00209-5.

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LEI, DERU, PEIYING CHEN, XUETING CHEN, YUJIE ZONG, and XIANGYANG LI. "Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry for Identification of Microorganisms in Clinical Urine Specimens after Two Pretreatments." Polish Journal of Microbiology 70, no. 2 (May 31, 2021): 207–13. http://dx.doi.org/10.33073/pjm-2021-018.

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Rapid identification of microorganisms in urine is essential for patients with urinary tract infections (UTIs). Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) has been proposed as a method for the direct identification of urinary pathogens. Our purpose was to compare centrifugation-based MALDI-TOF MS and short-term culture combined with MALDI-TOF MS for the direct identification of pathogens in urine specimens. We collected 965 urine specimens from patients with suspected UTIs, 211/965 isolates were identified as positive by conventional urine culture. Compared with the conventional method, the results of centrifugation-based MALDI-TOF MS were consistent in 159/211 cases (75.4%), of which 135/159 (84.9%) had scores ≥ 2.00; 182/211 cases (86.3%) were detected using short-term culture combined with MALDI-TOF MS, of which 153/182 (84.1%) had scores ≥ 2.00. There were no apparent differences among the three methods (p = 0.135). MALDI-TOF MS appears to accelerate the microbial identification speed in urine and saves at least 24 to 48 hours compared with the routine urine culture. Centrifugation-based MALDI-TOF MS is characterized by faster identification speed; however, it is substantially affected by the number of bacterial colonies. In contrast, short-term culture combined with MALDI-TOF MS has a higher detection rate but a relatively slow identification speed. Combining these characteristics, the two methods may be effective and reliable alternatives to traditional urine culture.

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Elbehiry, Ayman, Musaad Aldubaib, Adil Abalkhail, Eman Marzouk, Ahmad ALbeloushi, Ihab Moussa, Mai Ibrahem, et al. "How MALDI-TOF Mass Spectrometry Technology Contributes to Microbial Infection Control in Healthcare Settings." Vaccines 10, no. 11 (November 8, 2022): 1881. http://dx.doi.org/10.3390/vaccines10111881.

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Healthcare settings have been utilizing matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) since 2010. MALDI-TOF MS has various benefits over the conventional method of biochemical identification, including ease of use, speed, accuracy, and low cost. This approach can solve many of the obstacles to identifying bacteria, fungi and viruses. As technology advanced, more and more databases kept track of spectra, allowing species with similar morphological, genotypic, and biochemical traits to be identified. Using MALDI-TOF MS for identification has become more accurate and quicker due to advances in sample preparation and database enrichment. Rapid sample detection and colony identification using MALDI-TOF MS have produced promising results. A key application of MALDI-TOF MS is quickly identifying highly virulent and drug-resistant diseases. Here, we present a review of the scientific literature assessing the effectiveness of MALDI-TOF MS for locating clinically relevant pathogenic bacteria, fungi, and viruses. MALDI-TOF MS is a useful strategy for locating clinical pathogens, however, it also has some drawbacks. A small number of spectra in the database and inherent similarities among organisms can make it difficult to distinguish between different species, which can result in misidentifications. The majority of the time additional testing may correct these problems, which happen very seldom. In conclusion, infectious illness diagnosis and clinical care are being revolutionized by the use of MALDI-TOF MS in the clinical microbiology laboratory.

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Sun, Zhen, Eric W. Findsen, and Dragan Isailovic. "Atmospheric pressure visible-wavelength MALDI-MS." International Journal of Mass Spectrometry 315 (April 2012): 66–73. http://dx.doi.org/10.1016/j.ijms.2012.03.002.

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Zhong, Xiao Yan, and Wolfgang Holzgreve. "MALDI-TOF MS in Prenatal Genomics." Transfusion Medicine and Hemotherapy 36, no. 4 (2009): 263–72. http://dx.doi.org/10.1159/000223098.

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Kuck, Dietmar, and Jörg W. Metzger. "ESI-, MALDI-, ICR- und “NW-MS”." Nachrichten aus Chemie, Technik und Laboratorium 43, no. 10 (October 1995): 1060–61. http://dx.doi.org/10.1002/nadc.19950431011.

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SATO, Hiroaki, and Hajime OHTANI. "MALDI-MS/MS-Structural Characterization of Polymers Beyond the Mass Determination." Kobunshi 55, no. 11 (2006): 897–901. http://dx.doi.org/10.1295/kobunshi.55.897.

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Nakamura, Masahiro, Marina Moritsuna, Keita Yuda, Shunsuke Fujimura, Yuki Sugiura, Shuichi Shimma, Koshiro Nishimoto, et al. "Quantitative MALDI-MS/MS assay for serum cortisol through charged derivatization." Journal of Pharmaceutical and Biomedical Analysis 178 (January 2020): 112912. http://dx.doi.org/10.1016/j.jpba.2019.112912.

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Westblade, Lars F., Omai B. Garner, Karen MacDonald, Constance Bradford, David H. Pincus, A. Brian Mochon, Rebecca Jennemann, et al. "Assessment of Reproducibility of Matrix-Assisted Laser Desorption Ionization–Time of Flight Mass Spectrometry for Bacterial and Yeast Identification." Journal of Clinical Microbiology 53, no. 7 (April 29, 2015): 2349–52. http://dx.doi.org/10.1128/jcm.00187-15.

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Matrix-assisted laser desorption ionization–time of flight (MALDI-TOF) mass spectrometry (MS) has revolutionized the identification of clinical bacterial and yeast isolates. However, data describing the reproducibility of MALDI-TOF MS for microbial identification are scarce. In this study, we show that MALDI-TOF MS-based microbial identification is highly reproducible and can tolerate numerous variables, including differences in testing environments, instruments, operators, reagent lots, and sample positioning patterns. Finally, we reveal that samples of bacterial and yeast isolates prepared for MALDI-TOF MS identification can be repeatedly analyzed without compromising organism identification.

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Beganovic, Maya, Michael Costello, and Sarah M. Wieczorkiewicz. "Effect of Matrix-Assisted Laser Desorption Ionization–Time of Flight Mass Spectrometry (MALDI-TOF MS) Alone versus MALDI-TOF MS Combined with Real-Time Antimicrobial Stewardship Interventions on Time to Optimal Antimicrobial Therapy in Patients with Positive Blood Cultures." Journal of Clinical Microbiology 55, no. 5 (February 22, 2017): 1437–45. http://dx.doi.org/10.1128/jcm.02245-16.

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ABSTRACT Matrix-assisted laser desorption ionization–time of flight mass spectrometry (MALDI-TOF MS) decreases the time to organism identification and improves clinical and financial outcomes. The purpose of this study was to evaluate the impact of MALDI-TOF MS alone versus MALDI-TOF MS combined with real-time, pharmacist-driven, antimicrobial stewardship (AMS) intervention on patient outcomes. This single-center, pre-post, quasiexperimental study evaluated hospitalized patients with positive blood cultures identified via MALDI-TOF MS combined with prospective AMS intervention compared to a control cohort with MALDI-TOF MS identification without AMS intervention. AMS intervention included: real-time MALDI-TOF MS pharmacist notification and prospective AMS provider feedback. The primary outcome was the time to optimal therapy (TTOT). A total of 252 blood cultures, 126 in each group, were included in the final analysis. MALDI-TOF MS plus AMS intervention significantly reduced the overall TTOT (75.17 versus 43.06 h; P < 0.001), the Gram-positive contaminant TTOT (48.21 versus 11.75 h; P < 0.001), the Gram-negative infection (GNI) TTOT (71.83 versus 35.98 h; P < 0.001), and the overall hospital length of stay (LOS; 15.03 versus 9.02 days; P = 0.021). The TTOT for Gram-positive infection (GPI) was improved (64.04 versus 41.61 h; P = 0.082). For GPI, the hospital LOS (14.64 versus 10.31 days; P = 0.002) and length of antimicrobial therapy 24.30 versus 18.97 days; P = 0.018) were reduced. For GNI, the time to microbiologic clearance (51.13 versus 34.51 h; P < 0.001), the hospital LOS (15.40 versus 7.90 days; P = 0.027), and the intensive care unit LOS (5.55 versus 1.19 days; P = 0.035) were reduced. To achieve optimal outcomes, rapid identification with MALDI-TOF MS combined with real-time AMS intervention is more impactful than MALDI-TOF MS alone.

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Gundry, Rebekah L., Roy Edward, Thomas P. Kole, Chris Sutton, and Robert J. Cotter. "Disposable Hydrophobic Surface on MALDI Targets for Enhancing MS and MS/MS Data of Peptides." Analytical Chemistry 77, no. 20 (October 2005): 6609–17. http://dx.doi.org/10.1021/ac050500g.

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Gustafsson, Johan O. R., James S. Eddes, Stephan Meding, Tomas Koudelka, Martin K. Oehler, Shaun R. McColl, and Peter Hoffmann. "Internal calibrants allow high accuracy peptide matching between MALDI imaging MS and LC-MS/MS." Journal of Proteomics 75, no. 16 (August 2012): 5093–105. http://dx.doi.org/10.1016/j.jprot.2012.04.054.

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André, Magali, Jean-Pierre Le Caer, Céline Greco, Sébastien Planchon, Wassim El Nemer, Claude Boucheix, Eric Rubinstein, Julia Chamot-Rooke, and François Le Naour. "Proteomic analysis of the tetraspanin web using LC-ESI-MS/MS and MALDI-FTICR-MS." PROTEOMICS 6, no. 5 (March 2006): 1437–49. http://dx.doi.org/10.1002/pmic.200500180.

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Hortin, Glen L. "The MALDI-TOF Mass Spectrometric View of the Plasma Proteome and Peptidome." Clinical Chemistry 52, no. 7 (July 1, 2006): 1223–37. http://dx.doi.org/10.1373/clinchem.2006.069252.

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Abstract Background: Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and the related technique, surface-enhanced laser desorption/ionization (SELDI)-TOF MS, are being applied widely to analyze serum or plasma specimens for potential disease markers. Methods: Reports on the basic principles and applications of MALDI-TOF MS were reviewed and related to information on abundance and masses of major plasma proteins. Outcomes: MALDI-TOF MS is a particle-counting method that responds to molar abundance, and ranking of plasma proteins by molar abundance increases the rank of small proteins relative to traditional ranking by mass abundance. Detectors for MALDI-TOF MS augment the bias for detecting smaller components by yielding stronger signals for an equivalent number of small vs large ions. Consequently, MALDI-TOF MS is a powerful tool for surveying small proteins and peptides comprising the peptidome or fragmentome, opening this new realm for analysis. It is complementary to techniques such as electrophoresis and HPLC, which have a bias for detecting larger molecules. Virtually all of the potential markers identified by MALDI-TOF MS to date represent forms of the most abundant plasma proteins. Conclusions: Analyses of serum or plasma by MALDI-TOF MS provide new information mainly about small proteins and peptides with high molar abundance. The spectrum of observed proteins and peptides suggests value for applications such as assessment of cardiovascular risk, nutritional status, liver injury, kidney failure, and systemic immune responses rather than early detection of cancer. Extending analysis by MALDI-TOF MS to lower abundance components, such as markers for early-stage cancers, probably will require more extensive specimen fractionation before analysis.

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Tsuchida, Sachio, Hiroshi Umemura, and Tomohiro Nakayama. "Current Status of Matrix-Assisted Laser Desorption/Ionization–Time-of-Flight Mass Spectrometry (MALDI-TOF MS) in Clinical Diagnostic Microbiology." Molecules 25, no. 20 (October 17, 2020): 4775. http://dx.doi.org/10.3390/molecules25204775.

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Mass spectrometry (MS), a core technology for proteomics and metabolomics, is currently being developed for clinical applications. The identification of microorganisms in clinical samples using matrix-assisted laser desorption/ionization–time-of-flight mass spectrometry (MALDI-TOF MS) is a representative MS-based proteomics application that is relevant to daily clinical practice. This technology has the advantages of convenience, speed, and accuracy when compared with conventional biochemical methods. MALDI-TOF MS can shorten the time used for microbial identification by about 1 day in routine workflows. Sample preparation from microbial colonies has been improved, increasing the accuracy and speed of identification. MALDI-TOF MS is also used for testing blood, cerebrospinal fluid, and urine, because it can directly identify the microorganisms in these liquid samples without prior culture or subculture. Thus, MALDI-TOF MS has the potential to improve patient prognosis and decrease the length of hospitalization and is therefore currently considered an essential tool in clinical microbiology. Furthermore, MALDI-TOF MS is currently being combined with other technologies, such as flow cytometry, to expand the scope of clinical applications.

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Fresnais, Margaux, Esra Yildirim, Seda Karabulut, Dirk Jäger, Inka Zörnig, Julia Benzel, Kristian W. Pajtler, et al. "Rapid MALDI-MS Assays for Drug Quantification in Biological Matrices: Lessons Learned, New Developments, and Future Perspectives." Molecules 26, no. 5 (February 26, 2021): 1281. http://dx.doi.org/10.3390/molecules26051281.

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Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has rarely been used in the field of therapeutic drug monitoring, partly because of the complexity of the ionization processes between the compounds to be quantified and the many MALDI matrices available. The development of a viable MALDI-MS method that meets regulatory guidelines for bioanalytical method validation requires prior knowledge of the suitability of (i) the MALDI matrix with the analyte class and properties for ionization, (ii) the crystallization properties of the MALDI matrix with automation features, and (iii) the MS instrumentation used to achieve sensitive and specific measurements in order to determine low pharmacological drug concentrations in biological matrices. In the present hybrid article/white paper, we review the developments required for the establishment of MALDI-MS assays for the quantification of drugs in tissues and plasma, illustrated with concrete results for the different steps. We summarize the necessary parameters that need to be controlled for the successful development of fully validated MALDI-MS methods according to regulatory authorities, as well as currently unsolved problems and promising ways to address them. Finally, we propose an expert opinion on future perspectives and needs in order to establish MALDI-MS as a universal method for therapeutic drug monitoring.

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Felder, Thorsten, Christoph A. Schalley, Hassan Fakhrnabavi, and Oleg Lukin. "A Combined ESI- and MALDI-MS(/MS) Study of Peripherally Persulfonylated Dendrimers: False Negative Results by MALDI-MS and Analysis of Defects." Chemistry - A European Journal 11, no. 19 (September 19, 2005): 5625–36. http://dx.doi.org/10.1002/chem.200401236.

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