​ MODEL A+ expands B2B product portfolios in fastest-growing B-segment SUV MODEL K+ SUV playful styling gives nostalgic touches of Japan with neo city pop MODEL K taps into kei-class trucks with design language of MODEL T Flexing CDMS strength to accelerate electromobility for automotive clients TAIPEI, Oct. 30, 2026 /PRNewswire/ -- Hon Hai Technology Group (Foxconn) (TWSE: 2317) on Friday flexed its contract design and manufacturing service (CDMS) strength for automotive clients by unveiling three new reference electric vehicles aimed at under-penetrated markets, while offering cost competitive options and flexible design platforms. 

Higher-order antibody aggregates remain challenging to characterize using conventional mass spectrometry because of their low abundance, broad mass distributions, and extensive heterogeneity. Here, the practical performance of a commercial electrostatic linear ion trap charge detection mass spectrometer (XevoTM CDMS) was evaluated for therapeutic antibody analysis. The platform provided reproducible mass and charge measurements, with repeatability and intermediate-precision RSDs below 1%, and maintained consistent mass determination across the concentration and solution conditions examined. Controlled mixtures of antibody-derived species showed a linear molar-ratio-dependent ion response, supporting semi-quantitative estimation of relative species abundance under defined conditions. For heat-stressed trastuzumab, CDMS measurements were qualitatively consistent with SEC-MALS, mass photometry, and conventional native MS, while enabling direct mass determination of individual ions within highly heterogeneous high-molecular-weight (HMW) populations that exhibited extensive charge-state overlap and could not be reliably deconvoluted by conventional native MS. High-duty-cycle acquisition increased sampling of low-abundance, high-m/z ions and improved access to higher-order aggregate signals. Joint single ion mass-charge analysis further differentiated statistical ion families within the broad HMW fraction and related major mass differences to independently obtained compositional information. These results support commercial XevoTM CDMS as a practical multidimensional platform for antibody aggregate characterization.

AbstractThe clinical success of messenger ribonucleic acid (mRNA) therapeutics has driven the need for robust analytical techniques capable of characterizing mixtures of megadalton (MDa) constructs. A critical attribute of these therapeutics is the presence and length of the 3′ poly(A) tail, which governs mRNA stability and translational efficiency. Charge detection mass spectrometry (CDMS) was used to distinguish and quantify intact MDa mRNA variants differing only by the poly(A) content. Initial analysis under native-like conditions was limited by salt adduction, but a 75% methanol solution resulted in nearly a five-fold increase in charge (from ∼60e to ∼280e) and substantially less adduction. Measured masses of the intact mRNA were 1.054 MDa and 1.027 MDa for the tailed and non-tailed mRNA constructs, respectively, consistent with the theoretical 26.6 kDa mass difference. Mixtures of various compositions resulted in broad, unresolved peaks at intermediate mass owing to residual salt adduction. A constrained Gaussian deconvolution of these data enabled accurate quantification across seven different mole fractions (R2 = 0.978). Notably, an analysis of a subpopulation of the highest charge-state ions revealed separation into two distinct peaks, demonstrating that mass resolution for MDa mRNA analysis is limited by adduction rather than instrumental factors, motivating additional studies on methods to increase charging for more accurate quantification. These results establish CDMS as a powerful, top-down method for precise monitoring of mRNA heterogeneity and degradation in high molecular weight therapeutics.

An integrated analytical strategy combining CDMS and native digestion was used to study AAV stability under thermal stress, revealing diverse degradation products arising from cooperative DNA ejection and VP1u externalization. Tethering between ejected DNA and externalized viral protein promoted large aggregate formation, which was confirmed by native enzyme treatment.

Proteins have been often assumed to recognize interaction partners one amino-acid residue at a time. Jiang et al. introduce a computational and experimental platform that systematically captures epistatic, non-linearities (multiple amino-acid residues acting synergistically) in protein interactions. They uncover super-binding peptides and molecular determinants of non-linear binding from combinatorial deep mutational scanning (CDMS) libraries.