Development of a mertansine-specific DNA aptamer and novel high-throughput sandwich enzyme-linked oligonucleotide assay for quantification and characterization of trastuzumab emtansine.

We developed a novel DNA aptamer, D8#24S1, which specifically recognizes mertansine (DM1), the cytotoxic payload of the antibody-drug conjugate (ADC) trastuzumab emtansine (T-DM1), and applied it for T-DM1 analysis. D8#24S1 was obtained through SELEX and was shown to specifically recognize DM1 with high affinity (dissociation constant, K = 84.2 nM).

Effect of low-frequency acupuncture on muscle and fascia stiffness: examination with or without intervention.

Background: Low-frequency acupuncture is used to maintain skeletal muscle flexibility and improve joint range of motion; however, its definite effects are unclear. This study aimed to determine the effects of low-frequency acupuncture on muscle and fascial stiffness and ankle dorsiflexion range of motion.

Methods: The participants included 12 randomly selected healthy adults.

Simple and fast one-step FRET assay of therapeutic mAb bevacizumab using anti-idiotype DNA aptamer for process analytical technology.

We developed an aptamer-based fluorescence resonance energy transfer (FRET) assay capable of recognizing therapeutic monoclonal antibody bevacizumab and rapidly quantifying its concentration with just one mixing step. In this assay, two fluorescent dyes (fluorescein and tetramethylrhodamine) labeled aptamers bind to two Fab regions on bevacizumab, and FRET fluorescence is observed when both dyes come into close proximity. We optimized this assay in three different formats, catering to a wide range of analytical needs.

Development of a highly efficient solubilization method for mass spectrometric analysis of phospholipids in living single cells.

Phospholipids are vital constituents of the cell membrane and aid in signal transduction. Phospholipid profiles vary distinctively with the cell type. Notably, specific phospholipid molecules are present in significantly higher or lower concentrations in cancer cells versus normal cells.

Selective analysis of intracellular UDP-GlcNAc and UDP-GalNAc by hydrophilic interaction liquid chromatography-mass spectrometry.

Uridine diphosphate--acetylglucosamine (UDP-GlcNAc) is one of the major nucleotide sugars in living organisms and serves as the key donor substrate for the post-translational modification of protein -GlcNAcylation. It undergoes interconversion to its epimer uridine diphosphate--acetylgalactosamine (UDP-GalNAc), which acts as a sugar donor initiating mucin-type -linked glycosylation. The intracellular levels of the two differ between the cell lines and largely fluctuate in response to metabolic perturbations, and recent studies have focused on the details of their biosynthesis or turnover.