Two highly deuterium-labeled compounds, (R)-K-13675-d(11) and (R)-K-13675-d(7), were prepared for use as internal standards for low-level quantification of plasma drugs by LC/MS/MS. We successfully demonstrated their utility in pharmacokinetic studies for sensitive and precise drug quantification.
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http://dx.doi.org/10.1016/j.bmc.2009.01.049 | DOI Listing |
J Mater Chem B
January 2025
Chemical and Environmental Engineering, School of Engineering, STEM College, RMIT University, Melbourne, VIC 3000, Australia.
The controlled co-assembly of biomacromolecules through tuneable interactions offers a simple and fascinating opportunity to assemble multiple molecules into a single entity with enhanced complexity and unique properties. Herein, our study presents a dynamic co-assembled system using the multistimuli responsive intrinsically disordered protein Rec1-resilin and the adhesive hydrophilic protein silk sericin (SS). We utilized advanced characterization techniques including circular dichroism (CD) spectroscopy, dynamic light scattering (DLS), small-angle X-ray scattering (SAXS), and small/ultra-small angle neutron scattering (SANS/USANS) to elucidate the detailed co-assembly behavior of the system and its evolution over time and temperature.
View Article and Find Full Text PDFPharmaceuticals (Basel)
October 2024
Department of Nutritional, Food and Consumer Sciences, Fulda University of Applied Sciences, 36037 Fulda, Germany.
Our study presented a novel LC-MS/MS method for the simultaneous quantification of α-tocopherol (α-TOH) and its phase II metabolites, α-13'-COOH and α-13'-OH, in human serum using deuterium-labeled internal standards (d-α-TOH, d-α-13'-COOH, d-α-13'-OH). The method addresses the analytical challenge posed by the significantly different concentration ranges of α-TOH (µmol/L) and its metabolites (nmol/L). Previous methods quantified these analytes separately, which caused an increase in workflow complexity.
View Article and Find Full Text PDFJ Am Chem Soc
November 2024
Department of Biochemistry, Duke University School of Medicine, Durham, North Carolina 27710, United States.
Dynobactins are recently discovered ribosomally synthesized and post-translationally modified peptide (RiPP) antibiotics that selectively kill Gram-negative pathogens by inhibiting the β-barrel assembly machinery (Bam) located on their outer membranes. Such activity of dynobactins derives from their unique cross-links between Trp1-Asn4 and His6-Tyr8. In particular, the His6-Tyr8 cross-link is formed between N of His6 and C of Tyr8, an unprecedented type of cross-link in RiPP natural products.
View Article and Find Full Text PDFChemistry
September 2024
State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing, 100029, China.
The increasing demand for deuterium-labeled amino acids and derivatives has heightened interest in direct hydrogen/deuterium exchange reactions of free amino acids. Existing methods, including biocatalysis and metal catalysis, typically require expensive deuterium sources or excessive use of deuterium reagents and often struggle with site selectivity. In contrast, this binary catalysis system, employing benzaldehyde and CsCO in the presence of inexpensive DO with minimal stoichiometric quantities, facilitates efficient hydrogen/deuterium exchange at the α-position of amino acids without the need for protecting groups in the polar aprotic solvent DMSO.
View Article and Find Full Text PDFJACS Au
June 2024
College of Pharmacy, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 08826, Republic of Korea.
Deuterium-labeled α-amino acids are useful in research related to drug discovery and biomedical science. However, a high degree of site selectivity and stereoselectivity in the deuterium incorporation process is still difficult to achieve. Herein, we report a new enantioselective deuteration method at the α-position of several amino acids without external chiral sources.
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