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Journal articles on the topic 'MALDI'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Osa, Morichika, Maria Cecilia Belo, Zita Dela Merced, et al. "Performance of MALDI–TOF Mass Spectrometry in the Philippines." Tropical Medicine and Infectious Disease 6, no. 3 (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 hig

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2

KAWABATA, Shin-ichirou. "MALDI-TOFMS." Journal of the Japan Society of Colour Material 79, no. 6 (2006): 257–62. http://dx.doi.org/10.4011/shikizai1937.79.257.

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Kajiwara, Hideyuki. "MALDI biotyping." Nippon Shokuhin Kagaku Kogaku Kaishi 65, no. 11 (2018): 541. http://dx.doi.org/10.3136/nskkk.65.541.

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Wisztorski, Maxence, Rémi Lemaire, Jonathan Stauber, et al. "Imagerie MALDI." médecine/sciences 23 (March 2007): 31–38. http://dx.doi.org/10.1051/medsci/2007231s31.

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5

Chakrabarti, A. "MALDI-TOF." International Journal of Infectious Diseases 45 (April 2016): 26. http://dx.doi.org/10.1016/j.ijid.2016.02.090.

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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 (2016): 204–7. http://dx.doi.org/10.1177/2211068215594769.

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Rim, John Hoon, Yangsoon Lee, Sung Kuk Hong, et al. "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 isol

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Chen, Xin-Fei, Xin Hou, Meng Xiao, et al. "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 (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-

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Oluwatosin Ogundairo, Oluwatoyin Ayo-Farai, Chinedu Paschal Maduka, Chiamaka Chinaemelum Okongwu, Abdulraheem Olaide Babarinde, and Olamide Tolulope Sodamade. "REVIEW ON MALDI MASS SPECTROMETRY AND ITS APPLICATION IN CLINICAL RESEARCH." International Medical Science Research Journal 3, no. 3 (2023): 108–26. http://dx.doi.org/10.51594/imsrj.v3i3.642.

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Mass spectrometry has emerged as a powerful analytical tool in various scientific disciplines, and Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry (MALDI-MS) has gained significant prominence, particularly in the field of clinical research. This review provides a comprehensive overview of MALDI-MS, its principles, and its applications in clinical research settings. This study delves into the technical aspects of MALDI-MS, discussing key components such as the matrix, sample preparation methods, and mass analyzers. It highlights recent advancements and innovations in MALDI-MS tech

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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 (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 gav

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Rodríguez-Sánchez, Belén, María Jesús Ruiz-Serrano, Mercedes Marín, Paula López Roa, Marta Rodríguez-Créixems, and Emilio Bouza. "Evaluation of Matrix-Assisted Laser Desorption Ionization–Time of Flight Mass Spectrometry for Identification of Nontuberculous Mycobacteria from Clinical Isolates." Journal of Clinical Microbiology 53, no. 8 (2015): 2737–40. http://dx.doi.org/10.1128/jcm.01380-15.

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Matrix-assisted laser desorption ionization–time of flight mass spectrometry (MALDI-TOF MS) for the identification of nontuberculous mycobacterial (NTM) isolates was evaluated in this study. Overall, 125 NTM isolates were analyzed by MALDI-TOF and GenoType CM/AS. Identification by 16S rRNA/hsp65sequencing was considered the gold standard. Agreements between MALDI-TOF and GenoType CM/AS with the reference method were, respectively, 94.4% and 84.0%. In 17 cases (13.6%), results provided by GenoType and MALDI-TOF were discordant; however, the reference method agreed with MALDI-TOF in 16/17 cases

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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)

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Ulshina, D. V., D. A. Kovalev, D. G. Ponomarenko, et al. "APPLICATION OF TIME-OF-FLIGHT MASS-SPECTROMETRY FOR DETECTION OF CAUSATIVE AGENT OF BRUCELLOSIS IN BLOOD SAMPLES IN EXPERIMENT." Journal of microbiology epidemiology immunobiology, no. 4 (August 28, 2017): 9–17. http://dx.doi.org/10.36233/0372-9311-2017-4-9-17.

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Aim.Study the possibility to apply time-of-flight mass-spectrometry for detection of causative agent of brucellosis in blood. Materials and methods. Brucella strains: 5 Brucella melitensis and 21 Brucella abortus. Protein profiling in linear mode on MALD1-TOF mass-spectrometer Microflex «Bruker Daltonics». Results. Technique for disinfection and preparation of blood samples was modified and optimized for MALDI-TOF MS analysis. 120 representative protein profiles of sera extract were obtained that contain brucellosis causative agent. A resulting peak-list (super-spectrum) of the studied protein

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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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15

Kriegsmann, J., R. Casadonte, F. Zweynert, M. Kriegsmann, M. Otto, and S. Deininger. "MALDI-TOF-Bildgebung." Zeitschrift für Rheumatologie 72, no. 7 (2013): 724–28. http://dx.doi.org/10.1007/s00393-013-1239-1.

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Qiao, Hui, Gamini Piyadasa, Victor Spicer, and Werner Ens. "Analyte distributions in MALDI samples using MALDI imaging mass spectrometry." International Journal of Mass Spectrometry 281, no. 1-2 (2009): 41–51. http://dx.doi.org/10.1016/j.ijms.2008.11.015.

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De Waele, Gaetan, Gerben Menschaert, Peter Vandamme, and Willem Waegeman. "Pre-trained Maldi Transformers improve MALDI-TOF MS-based prediction." Computers in Biology and Medicine 186 (March 2025): 109695. https://doi.org/10.1016/j.compbiomed.2025.109695.

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18

Dickinson, Danielle N., Myron T. La Duc, William E. Haskins, et al. "Species Differentiation of a Diverse Suite of Bacillus Spores by Mass Spectrometry-Based Protein Profiling." Applied and Environmental Microbiology 70, no. 1 (2004): 475–82. http://dx.doi.org/10.1128/aem.70.1.475-482.2004.

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ABSTRACT In this study, we demonstrate the versatility of matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOFMS) protein profiling for the species differentiation of a diverse suite of Bacillus spores. MALDI-TOFMS protein profiles of 11 different strains of Bacillus spores, encompassing nine different species, were evaluated. Bacillus species selected for MALDI-TOFMS analysis represented the spore-forming bacterial diversity of typical class 100K clean room spacecraft assembly facilities. A one-step sample treatment and MALDI-TOFMS preparation were used to m

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Darie-Ion, Laura, Danielle Whitham, Madhuri Jayathirtha, et al. "Applications of MALDI-MS/MS-Based Proteomics in Biomedical Research." Molecules 27, no. 19 (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 ti

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Fresnais, Margaux, Esra Yildirim, Seda Karabulut, et al. "Rapid MALDI-MS Assays for Drug Quantification in Biological Matrices: Lessons Learned, New Developments, and Future Perspectives." Molecules 26, no. 5 (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 (

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Albrethsen, Jakob. "Reproducibility in Protein Profiling by MALDI-TOF Mass Spectrometry." Clinical Chemistry 53, no. 5 (2007): 852–58. http://dx.doi.org/10.1373/clinchem.2006.082644.

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Abstract Background: Protein profiling with high-throughput sample preparation and MALDI-TOF MS analysis is a new potential tool for diagnosis of human diseases. However, analytical reproducibility is a significant challenge in MALDI protein profiling. This minireview summarizes studies of reproducibility of MALDI protein profiling and current approaches to improve its analytical performance. Methods: The PubMed database was searched using combinations of the following search terms: MALDI, SELDI, reproducibility, variation, precision, peak intensity, quantification, peptide, biomarkers, and pr

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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 (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

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Ellis, S. R., J. Soltwisch, M. R. L. Paine, K. Dreisewerd, and R. M. A. Heeren. "Laser post-ionisation combined with a high resolving power orbitrap mass spectrometer for enhanced MALDI-MS imaging of lipids." Chemical Communications 53, no. 53 (2017): 7246–49. http://dx.doi.org/10.1039/c7cc02325a.

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Coupling laser post-ionisation with a high resolving power MALDI Orbitrap mass spectrometer has realised an up to ∼100-fold increase in the sensitivity and enhanced the chemical coverage for MALDI-MS imaging of lipids relative to conventional MALDI.

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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

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Beeman, Katrin, Jens Baumgärtner, Manuel Laubenheimer, et al. "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 (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 enzyma

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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 (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 micr

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Sousa, Roberto B., Keila S. C. Lima, Caleb G. M. Santos, et al. "A New Method for Extraction and Analysis of Ricin Samples through MALDI-TOF-MS/MS." Toxins 11, no. 4 (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 i

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Montaudo, Giorgio, Filippo Samperi, Maurizio S. Montaudo, Sabrina Carroccio, and Concetto Puglisi. "Current Trends in Matrix-Assisted Laser Desorption/Ionization of Polymeric Materials." European Journal of Mass Spectrometry 11, no. 1 (2005): 1–14. http://dx.doi.org/10.1255/ejms.718.

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In the last few years, mass spectrometry has rapidly become indispensable in polymer analysis and complements, in many ways, the structural data provided by nuclear magnetic resonance. Mass spectrometry of polymers is emerging as a revolutionary technique, capable of challenging the techniques and protocols established for years for the characterization of synthetic polymers. Matrix-assisted laser desorption/ionization (MALDI) has become a widely applied method for the structural characterization of synthetic polymers. The primary aim of this review is to illustrate some recent advances in the

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Neuenschwander, Felix R., Birgit Groß, and Sören Schubert. "Rapid Antibiotic Susceptibility Testing of Gram-Negative Bacteria Directly from Urine Samples of UTI Patients Using MALDI-TOF MS." Antibiotics 12, no. 6 (2023): 1042. http://dx.doi.org/10.3390/antibiotics12061042.

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Urinary tract infections (UTIs) are one of the most common human infections and are most often caused by Gram-negative bacteria such as Escherichia coli. In view of the increasing number of antibiotic-resistant isolates, rapidly initiating effective antibiotic therapy is essential. Therefore, a faster antibiotic susceptibility test (AST) is desirable. The MALDI-TOF MS-based phenotypic antibiotic susceptibility test (MALDI AST) has been used in blood culture diagnostics to rapidly detect antibiotic susceptibility. This study demonstrates for the first time that MALDI AST can be used to rapidly

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Ogundairo, Oluwatosin, Oluwatoyin Ayo Farai, Chinedu Paschal Maduka, Chiamaka Chinaemelum Okongwu, Abdulraheem Olaide Babarinde, and Olamide Tolulope Sodamade. "Review on MALDI Imaging for Direct Tissue Imaging and its Application in Pharmaceutical Research." International Journal of Research and Scientific Innovation X, no. XII (2024): 130–41. http://dx.doi.org/10.51244/ijrsi.2023.1012011.

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Matrix-Assisted Laser Desorption/Ionization (MALDI) imaging has emerged as a powerful analytical technique, enabling direct tissue imaging in pharmaceutical research. This review provides an in-depth exploration of the principles, methodologies, and applications of MALDI imaging in the context of studying drug distribution and molecular changes within tissues. provides a structured approach to exploring the principles, methodologies, applications, challenges, and future directions of MALDI Imaging in pharmaceutical research. Each section aims to contribute to a comprehensive understanding of t

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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 (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 ag

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Lippa, Timothy, Nelli I. Taranenko, Coorg R. Prasad, and Vladimir M. Doroshenko. "Infrared Matrix-Assisted Laser Desorption/Ionization Quadrupole Ion Trap Mass Spectrometry." European Journal of Mass Spectrometry 8, no. 3 (2002): 263–71. http://dx.doi.org/10.1255/ejms.498.

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Performance characteristics of an infrared (IR) matrix-assisted laser desorption/ionization (MALDI) quadrupole ion trap (QIT) mass spectrometer are presented. Both an IR laser and an ultraviolet (UV) laser have been coupled to the MALDI ion source, allowing for a comparative study of the spectra obtained for the same analyte molecules taken at these two wavelengths. The mass range of the QIT instrument was extended by operating it at a frequency as low as 200 kHz. The results presented for small and medium-size peptides demonstrated a lesser degree of analyte ion fragmentation in the case of t

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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 (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

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Jagannadham, Medicharla V., and Ramakrishnan Nagaraj. "Detecting the Site of Phosphorylation in Phosphopeptides without Loss of Phosphate Group Using MALDI TOF Mass Spectrometry." Analytical Chemistry Insights 3 (January 2008): ACI.S497. http://dx.doi.org/10.4137/aci.s497.

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Phosphopeptides with one and four phosphate groups were characterized by MALDI mass spectrometry. The molecular ion of monophosphopeptide could be detected both as positive and negative ions by MALDI TOF with delayed extraction (DE) and in the reflector mode. The tetraphospho peptide could be detected in linear mode. When MS/MS spectra of the monophospho peptides were obtained in a MALDI TOF TOF instrument by CID, b and y ions with the intact phosphate group were observed, in addition the b and y ions without the phosphate group. Our study indicates that it is possible to detect phosphorylated

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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 (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 cultu

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Elbehiry, Ayman, Musaad Aldubaib, Adil Abalkhail, et al. "How MALDI-TOF Mass Spectrometry Technology Contributes to Microbial Infection Control in Healthcare Settings." Vaccines 10, no. 11 (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 m

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Berg, H. E., S. Shannon, and A. N. Schuetz. "Anaerobes Direct from Blood Culture Bottles Can Be Identified by Early Matrix-Assisted Laser Desorption Ionization/ Time-of-Flight Mass Spectrometry (MALDI-TOF MS) at 24 Hours or Less." American Journal of Clinical Pathology 154, Supplement_1 (2020): S126. http://dx.doi.org/10.1093/ajcp/aqaa161.276.

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Abstract Introduction/Objective Matrix-assisted laser desorption ionization/ time-of-flight mass spectrometry (MALDI-TOF MS) direct from positive blood culture bottles has facilitated drastic drops in turn-around times for microorganism identification but has been poorly studied for anaerobes. We investigated the ability of MALDI-TOF to provide early anaerobe identification at 4 hours and 18-24 hours of growth on agar from anaerobic blood culture bottles. Additionally, we reviewed medical records of such patients to ascertain impact of early identification on antimicrobial treatment. Methods O

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Sparvero, Louis J., Andrew A. Amoscato, C. Edward Dixon, et al. "Mapping of phospholipids by MALDI imaging (MALDI-MSI): realities and expectations." Chemistry and Physics of Lipids 165, no. 5 (2012): 545–62. http://dx.doi.org/10.1016/j.chemphyslip.2012.06.001.

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Westblade, Lars F., Omai B. Garner, Karen MacDonald, 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 (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 f

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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 (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 co

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Chui, Huixia, Michael Chan, Drexler Hernandez, 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 (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 ma

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Martic, Sanela, John D. Brennan, Michael A. Brook, Suzanne Ackloo, and Noemi Nagy. "Towards the development of a covalently tethered MALDI system — A study of allyl-modified MALDI matrixes." Canadian Journal of Chemistry 85, no. 1 (2007): 66–76. http://dx.doi.org/10.1139/v06-185.

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An emerging application of matrix-assisted laser desorption ionization (MALDI) mass spectrometry is the analysis of low molecular weight (LMW) compounds, often via coupled liquid chromatography — MALDI-MS methods. However, in many cases, the low molecular weight region of MALDI mass spectra is obscured by the presence of signals originating from the matrix, suggesting that the development of tethered MALDI matrixes may be required to optimize MS performance for such compounds. To gain insight into potential sites for covalent attachment of MALDI matrixes, we have systematically investigated th

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Gorbunov A. Yu. and Podolskaya E. P. "Fabrication of nanoscale multimolecular structures of lanthanum stearate using Langmuir monolayers for laser desorption/ionization mass spectrometry." Technical Physics Letters 48, no. 11 (2022): 29. http://dx.doi.org/10.21883/tpl.2022.11.54885.19320.

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Matrix-assisted laser desorption/ionization (MALDI) from the surface of nanosized multimolecular structures based on lanthanum stearate monolayers (FLa) has been studied. The presence of FLa on the surface of MALDI target was confirmed experimentally by laser desorption of lanthanum-containing organic ions. MALDI target functionalization with FLa is shown to significantly increase the yield of target peptide ions, with the optimum being achieved at a film thickness of about 6 monolayers. An approach is proposed in a &quot;lab-on-a-plate&quot; format, which allows specific extraction of

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Barborini, Emanuele, Giacomo Bertolini, Monica Epifanio, Alexander Yavorskyy, Simone Vinati, and Marc Baumann. "Cluster-Assembled Nanoporous Super-Hydrophilic Smart Surfaces for On-Target Capturing and Processing of Biological Samples for Multi-Dimensional MALDI-MS." Molecules 27, no. 13 (2022): 4237. http://dx.doi.org/10.3390/molecules27134237.

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Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) on cluster-assembled super-hydrophilic nanoporous titania films deposited on hydrophobic conductive-polymer substrates feature a unique combination of surface properties that significantly improve the possibilities of capturing and processing biological samples before and during the MALDI-MS analysis without changing the selected sample target (multi-dimensional MALDI-MS). In contrast to pure hydrophobic surfaces, such films promote a remarkable biologically active film porosity at the nanoscale due to the soft assembling

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Bowman, Andrew P., James Sawicki, Nari N. Talaty, Wayne R. Buck, Junhai Yang, and David S. Wagner. "Evaluation of Quantitative Platforms for Single Target Mass Spectrometry Imaging." Pharmaceuticals 15, no. 10 (2022): 1180. http://dx.doi.org/10.3390/ph15101180.

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(1) Imaging of pharmaceutical compounds in tissue is an increasingly important subsection of Mass Spectrometry Imaging (MSI). Identifying proper target engagement requires MS platforms with high sensitivity and spatial resolution. Three prominent categories of drugs are small molecule drugs, antibody-drug conjugate payloads, and protein degraders. (2) We tested six common MSI platforms for their limit of detection (LoD) on a representative compound for each category: a Matrix-Assisted Laser Desorption/Ionization (MALDI) Fourier Transform Ion Cyclotron, a MALDI-2 Time-of-Flight (ToF), a MALDI-2

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Paziani, Mario Henrique, Ludmilla Tonani Carvalho, Marcia de Souza Carvalho Melhem, et al. "First Comprehensive Report of Clinical Fusarium Strains Isolated in the State of Sao Paulo (Brazil) and Identified by MALDI-TOF MS and Molecular Biology." Microorganisms 8, no. 1 (2019): 66. http://dx.doi.org/10.3390/microorganisms8010066.

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The aim of this study was to compare the performance of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), phenotypic and molecular methods for the identification of Fusarium species complexes isolated from clinical cases in the State of Sao Paulo (Brazil) between the years 2001 and 2017. Sequencing of ITS region of ribosomal DNA and elongation factor 1 alpha gene (ET1α) were used as reference method in the analysis of a total of 108 Fusarium spp. clinical strains isolated from human hosts with superficial and systemic infections. Agreement between MAL

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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 examine

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Harju, Inka, Christoph Lange, Markus Kostrzewa, Thomas Maier, Kaisu Rantakokko-Jalava, and Marjo Haanperä. "Improved Differentiation of Streptococcus pneumoniae and Other S. mitis Group Streptococci by MALDI Biotyper Using an Improved MALDI Biotyper Database Content and a Novel Result Interpretation Algorithm." Journal of Clinical Microbiology 55, no. 3 (2017): 914–22. http://dx.doi.org/10.1128/jcm.01990-16.

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ABSTRACTReliable distinction ofStreptococcus pneumoniaeand viridans group streptococci is important because of the different pathogenic properties of these organisms. Differentiation betweenS. pneumoniaeand closely relatedSreptococcusmitisspecies group streptococci has always been challenging, even when using such modern methods as 16S rRNA gene sequencing or matrix-assisted laser desorption ionization–time of flight (MALDI-TOF) mass spectrometry. In this study, a novel algorithm combined with an enhanced database was evaluated for differentiation betweenS. pneumoniaeandS. mitisspecies group s

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Murray, David L., John R. Mills, Maria Alice V. Willrich, David Barnidge, Mindy C. Kohlhagen, and Angela Dispenzieri. "A Rapid MALDI-TOF Method for Isotyping and Quantitating M-Proteins in a Single Assay: Longitudinal Comparison to Serum Protein Electrophoresis and Hevylite for Monitoring Patients with Monoclonal Gammopathies." Blood 126, no. 23 (2015): 1780. http://dx.doi.org/10.1182/blood.v126.23.1780.1780.

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Abstract Background: Current laboratory methods for detection of monoclonal gammopathies include a panel of serum protein electrophoresis (SPEP), immunofixation electrophoresis (IFE) and serum free light chain quantitation (FLC). Our group has recently described a new assay based on matrix assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry (MS) which is capable of detecting, isotyping and quantitating M-proteins in a single assay. The basic principle of the method involves leveraging the unique mass resulting from light chain (LC) Ig gene rearrangement in B-cells

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Sepiashvili, Lusia, Mindy C. Kohlhagen, Melissa R. Snyder, et al. "Direct Detection of Monoclonal Free Light Chains in Serum by Use of Immunoenrichment-Coupled MALDI-TOF Mass Spectrometry." Clinical Chemistry 65, no. 8 (2019): 1015–22. http://dx.doi.org/10.1373/clinchem.2018.299461.

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Abstract BACKGROUND Free light chain (FLC) quantification is the most analytically sensitive blood-based method commercially available to diagnose and monitor patients with plasma cell disorders (PCDs). However, instead of directly detecting monoclonal FLCs (mFLCs), FLC assays indirectly assess clonality based on quantifying κ and λ FLCs and determination of the к/λ FLC ratio. Often an abnormal FLC ratio is the only indication of a PCD, and confirmation by a direct method increases diagnostic confidence. The aim of this study was to develop an analytically sensitive method for direct detection

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