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Rapid separation of bile acid isomers via ion mobility mass spectrometry by complexing with spiramycin.
Anal Bioanal Chem
November 2024
Zhejiang Provincial Key Laboratory of Advanced Mass Spectrometry and Molecular Analysis, Institute of Mass Spectrometry, School of Material Science and Chemical Engineering, Ningbo University, Ningbo, 315211, Zhejiang, China.
Bile acid (BA) is one of the main active components of bile and has multiple isomers, the structure or content of its isomers often changes due to diseases and other health problems; thus, the accurate detection of BA isomers is very important. In this study, two groups of BA isomers of glycine-conjugated BAs and taurine-conjugated BAs were simultaneously separated and quantitatively analyzed by ion mobility mass spectrometry (IM-MS). Especially, baseline mobility separation between the isomers was achieved by the formation of binary complexes via simple interaction with spiramycin (SPM), for which a separation resolution (R) of 1.
View Article and Find Full Text PDFOptimized analysis for related substances in spiramycin based on high performance liquid chromatography with hybrid particle column and characterization of its impurities by single heartcut two-dimensional liquid chromatography coupled with quadrupole time-of-flight mass spectrometer.
J Pharm Biomed Anal
January 2025
Jiangsu Institute for Food and Drug Control, Nanjing 210019, China; NMPA Key Laboratory for Impurity Profile of Chemical Drugs, Nanjing 210019, China. Electronic address:
Article Synopsis
- The article discusses a new method for analyzing spiramycin-related substances using a hybrid particle column and specific chromatographic conditions.
- It employs two different mobile phases for gradient elution, resulting in a method that is characterized by strong specificity, sensitivity, and stability.
- Additionally, six previously unreported impurities above 0.1% were identified using advanced 2D liquid chromatography linked with a mass spectrometer (2D LC-QTOF-MS/MS).
Characteristics of acidic hydrothermal treatment for disintegration of spiramycin fermentation residue and degradation of residual antibiotics.
Bioresour Technol
October 2024
School of Environmental and Material Engineering, Yantai University, Yantai 264005, China. Electronic address:
To recycle the nutrients in spiramycin (SPM) fermentation residue (SFR) through biological methods, acid hydrothermal treatment (AHT) was employed as pretreatment to enhance SFR biodegradability. The results showed that the degradation rate of residual SPM in SFR reached 100% after 120 min at 100℃ and 0.30 M acid with a 30.
View Article and Find Full Text PDFSpiramycin-loaded maltodextrin nanoparticles as a promising treatment of toxoplasmosis on murine model.
Parasitol Res
July 2024
Department of Clinical and Molecular Parasitology, National Liver Institute, Menoufia University, Menoufia, Egypt.
Despite being the initial choice for treating toxoplasmosis, sulfadiazine and pyrimethamine have limited effectiveness in eliminating the infection and were linked to a variety of adverse effects. Therefore, the search for new effective therapeutic strategies against toxoplasmosis is still required. The current work is the first research to assess the efficacy of spiramycin-loaded maltodextrin nanoparticles (SPM-loaded MNPs) as a novel alternative drug therapy against toxoplasmosis in a murine model.
View Article and Find Full Text PDFThe global distribution of the macrolide esterase EstX from the alpha/beta hydrolase superfamily.
Commun Biol
June 2024
Antibiotics Research and Re-evaluation Key Laboratory of Sichuan Province, Sichuan Industrial Institute of Antibiotics, School of pharmacy, Chengdu University, 610106, Chengdu, China.
Macrolide antibiotics, pivotal in clinical therapeutics, are confronting resistance challenges mediated by enzymes like macrolide esterases, which are classified into Ere-type and the less studied Est-type. In this study, we provide the biochemical confirmation of EstX, an Est-type macrolide esterase that initially identified as unknown protein in the 1980s. EstX is capable of hydrolyzing four 16-membered ring macrolides, encompassing both veterinary (tylosin, tidipirosin, and tilmicosin) and human-use (leucomycin A5) antibiotics.
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