• Mass Spectrometry Letters
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• v.2 no.3
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• pp.61-64
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• 2011

Matrix Assisted Laser Desorption/Ionization-Time-of-Flight mass spectrometry (MALDI-TOF-MS) is the most widely used MS technique for glycan analysis. However, the poor point-to-point and sample-to-sample reproducibility becomes a limit in glycan biomarker research. A prespotted MALDI plate which overcomes the large crystal formation of 2,5-dihydroxybenzoic acid (DHB) has been developed and applied for glycan analysis. A homogeneous matrix coated surface without a crystal structure was formed on a hydrophilic/ hydrophobic patterned surface using a piezoelectric device. The reproducible MALDI-TOF-MS data have been presented using MALDI imaging of beer glycan as well as serum glycan eluted from 10% and 20% ACN elution fractions. The glycan profile from the serum glycan by MALDI-TOF-MS with a DHB prespotted plate was highly conserved for 10 different spectra and the coefficient of variations of significant ion peaks of MALDI data varies from 3.59 to 19.95.

• Korean Journal of Clinical Laboratory Science
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• v.55 no.4
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• pp.244-252
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• 2023

The timeliness and accuracy of test results are crucial factors for clinicians to decide and promptly administer effective and targeted antimicrobial therapy, especially in life-threatening infections or when vital organs and functions, such as sight, are at risk. Further research is needed to refine and optimize matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS)-based assays to obtain accurate and reliable results in the shortest time possible. MALDI-TOF MS-based bacterial identification focuses primarily on techniques for isolating and purifying pathogens from clinical samples, the expansion of spectral libraries, and the upgrading of software. As technology advances, many MALDI-based microbial identification databases and systems have been licensed and put into clinical use. Nevertheless, it is still necessary to develop MALDI-TOF MS-based antimicrobial-resistance analysis for comprehensive clinical microbiology characterization. The important applications of MALDI-TOF MS in clinical research include specific application categories, common analytes, main methods, limitations, and solutions. In order to utilize clinical microbiology laboratories, it is essential to secure expertise through education and training of clinical laboratory scientists, and database construction and experience must be maximized. In the future, MALDI-TOF mass spectrometry is expected to be applied in various fields through the use of more powerful databases.

• Mass Spectrometry Letters
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• v.5 no.2
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• pp.49-51
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• 2014

The effectiveness of tertiary matrices composed of the combination of three common matrices (dihydrobenzoic acid (DHB), ${\alpha}$-cyano-4-hydroxycinnamic acid (CHCA), and sinapinic acid (SA)) was compared with that of single or binary matrices in the analysis of polyethylene glycol (PEG) polymers ranging from 1400 to 10000 Da using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). A tertiary matrix of 2,5-DHB+CHCA+SA was the most effective in terms of S/N ratios. CHCA and CHCA+SA produced the highest S/N ratios among the single matrices and the binary matrices, respectively. The improvement observed when using a tertiary matrix in analyses of PEG polymers by MALDI-TOF MS is believed to be due to the uniform morphology of the MALDI sample spots and synergistic effects arising from the mixture of the three matrix materials.

• Bulletin of the Korean Chemical Society
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• v.28 no.12
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• pp.2354-2358
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• 2007

MALDI-TOF-MS technique was applied to obtain structural and compositional information of synthetic polyamides, Nylon6 and Nylon66. Mass spectra of both the original and the hydrolyzed polyamide samples were analyzed using the self calibration method as well as the internal calibration method with the standard materials of known masses. The MALDI-TOF mass spectra of Nylon6 samples showed the presence of protonated, sodiated, and potassiated ions that were assigned to cyclic and NH2/COOH terminated linear oligomers. From the MALDI-TOF mass spectra of Nylon66 samples, the potassiated linear oligomers with three different end groups are identified as well as the cyclic oligomers, i.e., NH2/COOH terminated oligomers, NH2/NH2 terminated oligomers, and COOH/COOH terminated oligomers. Full characterization of the molecular species and end groups present in the polyamide samples has been achieved, and also the changes in mass spectral patterns after the hydrolysis of the samples are presented.

• Mass Spectrometry Letters
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• v.6 no.3
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• pp.80-84
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• 2015

Here, we demonstrate the use of MALDI-TOF as a fast and simple analytical approach to evaluate the DNA-binding capability of various peptides. Specifically, by varying the amino acid sequence of the peptides consisting of lysine (K) and tryptophan (W), we identified peptides with strong DNA-binding capabilities using MALDI-TOF. Mass spectrometric analysis reveals an interesting novel finding that lysine residues show sequence selective preference, which used to be considered as mediator of electrostatic interactions with DNA phosphate backbones. Moreover, tryptophan residues show higher affinity to DNA than lysine residues. Since there are numerous possible combinations to make peptide oligomers, it is valuable to introduce a simple and reliable analytical approach in order to quickly identify DNA-binding peptides.

• Bulletin of the Korean Chemical Society
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• v.20 no.11
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• pp.1299-1302
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• 1999

Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) was used to demonstrate cross-linking of peptides induced by transglutaminase. The presence of ε-( Υ-glutamyl)lysine isopeptide cross-link in the acid hydrolysate of the cross-linking reaction mixture was also demonstrated by MALDI-TOF-MS without prior separation. MALDI-TOF-MS quickly provided peptide mass maps after pronase digestion of the cross-linked peptide adduct, which enabled us to monitor the hydrolytic sequence. Pronase appears to preferentially hydrolyze peptide bonds distant from the cross-link before hydrolyzing peptide bonds around the cross-link. The results suggest that pronase digestion followed by MALDI-TOF-MS could be used for determination of amino acid sequence around a modification site.

• Bulletin of the Korean Chemical Society
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• v.32 no.2
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• pp.477-482
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• 2011

The structural analysis of polytrimethylene terephthalate (PTT) and characterization of the hydrolytic degradation products after acid hydrolysis were performed using MALDI-TOF mass spectrometry. Mass spectra of the PTT samples were analyzed using a self-calibration method as well as an internal calibration method with standard materials of known masses. PTT structures constituting the samples were determined from the analyses of the spectra, and their relative compositions were estimated. The MALDI-TOF mass spectra of the acid-hydrolyzed PTT sample showed three main series of oligomer products with different end groups in accordance with the hydrolysis schemes. From the spectra of both $Na^+$ and $K^+$ adducts, it was concluded that the PTT samples have higher affinity for $Na^+$ compared with $K^+$ and therefore show higher ionization efficiency with sodium ions when dithranol is used as a matrix. Two different wavelength laser beams ($\lambda$ = 337 nm and 355 nm) were tested and it was observed that the 355 nm beam was more efficient in obtaining the MALDI spectra of PTT using dithranol as a matrix under our experimental conditions.

• Mass Spectrometry Letters
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• v.13 no.4
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• pp.106-114
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• 2022

A rapid and reliable approach to the identification of microorganisms is a critical requirement for large-scale culturomics analysis. MALDI-TOF MS is a suitable technique that can be a better alternative to conventional biochemical and gene sequencing methods as it is economical both in terms of cost and labor. In this review, the applications of MALDI-TOF MS for the comprehensive identification of microorganisms and bacterial strain typing for culturomics-based approaches for various environmental studies including bioremediation, plant sciences, agriculture and food microbiology have been widely explored. However, the restriction of this technique is attributed to insufficient coverage of the mass spectral database. To improve the applications of this technique for the identification of novel isolates, the spectral database should be updated with the peptide mass fingerprint (PMF) of type strains with not only microbes with clinical relevance but also from various environmental sources. Further, the development of enhanced sample processing methods and new algorithms for automation and de-replication of isolates will increase its application in microbial ecology studies.

• Korean Journal of Veterinary Service
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• v.39 no.4
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• pp.247-251
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• 2016

Salmonella is one of the most common bacteria that causes heavy losses in swine industry and major causative pathogen of food poisoning in public health. Various methods for the identification of Salmonella such as Gram staining, agglutination test, enzyme-linked immunosorbent assay (ELISA), polymerase chain reaction (PCR) have been used. Several studies have demonstrated that Matrix Assisted Laser Desorption Ionization Time of Flight (MALDI TOF) Mass Spectrometry (MS) identification is an efficient and inexpensive method for the rapid and routine identification of isolated bacteria. In this study, MALDI TOF MS could provide rapid, accurate identification of Salmonella spp. from swine compared with end point PCR and real time PCR.

• Bulletin of the Korean Chemical Society
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• v.33 no.3
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• pp.833-838
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• 2012

The thermal degradation products of polytrimethylene terephthalate (PTT) obtained by heating the sample in the temperature range of $250-360^{\circ}C$ under non-oxidative conditions was characterized using MALDI-TOF (matrix assisted laser desorption/ionization) mass spectrometry. The structures of the degradation products were determined and the relative compositions were estimated. The MALDI-TOF mass spectra of the thermally degraded PTT sample showed three main series of oligomer products with different end groups, which were carboxyl/carboxyl, carboxyl/allyl, and allyl/allyl. In contrast to the thermal degradation of polyethylene terephthalate (PET), the oligomers containing terephthalic anhydrides were not detected, whereas the formation of oligomers containing the unsaturated allyl ester group was confirmed by mass assignment. From these results, it was concluded that the thermal degradation of PTT proceeds exclusively through the ${\beta}$-CH hydrogen transfer mechanism, which is in accordance with the proposed reaction mechanism for the thermal degradation of polybutylene terephthalate (PBT).