RESUMEN
Designing advanced stationary phases to improve separation efficiency is essential in capillary electrochromatography. Due to their outstanding performance, covalent organic frameworks have recently demonstrated considerable promise in the field of separation science. Herein, an open-tubular capillary electrochromatography method was reported using porous imine-based covalent organic framework with sufficiently available interaction sites as stationary phase. The imine-based covalent organic framework coated capillary was easily prepared via an in situ growth method at room temperature, and its separation performance was evaluated, indicating the high separation efficiency for three types of analytes, including herbicides, polybrominated dibenzofurans, and bisphenols. Moreover, the imine-based covalent organic framework coated capillary showed good reproducibility and stability, with intraday (n = 3), interday (n = 3), and column-to-column (n = 3) relative standard deviations of retention time and peak areas of less than 5%. The separation efficiency of the coated capillary remained unchanged even after 200 runs and the maximum theoretical plates reached up to 85 595 N/m for 4,4'-ethylidenebisphenol. It was predicted that the imine-based covalent organic framework stationary phase would be a strong contender for chromatographic separation with high efficiency.
RESUMEN
Discrimination and quantification of amino acid (AA) enantiomers are particularly important for diagnosing and treating diseases. Recently, dual-mode probes have gained a lot of research interest because they can catch more detecting information compared with the single-mode probes. Thus, it is of great significance to develop a dual-mode sensor realizing AA enantiomer discrimination conveniently and efficiently. In this work, carbon dot L-TCDs were prepared by N-methyl-1,2-benzenediamine dihydrochloride (OTD) and l-tryptophan. With the assistance of H2O2, L-TCDs show an excellent discrimination performance for enantiomers of glutamine (Gln) and valine (Val) in both fluorescent and colorimetric modes. The fluorescence enantioselectivity of Gln (FD/FL) and Val (FL/FD) is 5.29 and 4.13, respectively, and the colorimetric enantioselectivity of Gln (ID/IL) and Val (IL/ID) is 13.26 and 3.42, individually. The chiral recognition mechanism of L-TCDs was systematically studied. L-TCDs can be etched by H2O2, and the participation of AA enantiomers results in different amounts of the released OTD, which provides fluorescent and colorimetric signals for identifying and quantifying the enantiomers of Gln and Val. This work provides a more convenient and flexible dual-mode sensing strategy for discriminating AA enantiomers, which is expected to be of great value in facile and high-throughput chiral recognition.
Asunto(s)
Glutamina , Valina , Colorimetría/métodos , Carbono/química , Peróxido de Hidrógeno , Aminoácidos , ColorantesRESUMEN
Although sulfonation plays crucial roles in various biological processes and is frequently utilized in medicinal chemistry to improve water solubility and chemical diversity of drug leads, it is rare and underexplored in ribosomally synthesized and post-translationally modiï¬ed peptides (RiPPs). Biosynthesis of RiPPs typically entails modification of hydrophilic residues, which substantially increases their chemical stability and bioactivity, albeit at the expense of reducing water solubility. To explore sulfonated RiPPs that may have improved solubility, we conducted co-occurrence analysis of RiPP class-defining enzymes and sulfotransferase (ST), and discovered two distinctive biosynthetic gene clusters (BGCs) encoding both lanthipeptide synthetase (LanM) and ST. Upon expressing these BGCs, we characterized the structures of novel sulfonated lanthipeptides and determined the catalytic details of LanM and ST. We demonstrate that SslST-catalyzed sulfonation is leader-independent but relies on the presence of A ring formed by LanM. Both LanM and ST are promiscuous towards residues in the A ring, but ST displays strict regioselectivity toward Tyr5. The recognition of cyclic peptide by ST was further discussed. Bioactivity evaluation underscores the significance of the ST-catalyzed sulfonation. This study sets up the starting point to engineering the novel lanthipeptide STs as biocatalysts for hydrophobic lanthipeptides improvement.