In the year 2003 there was a 17% increase in the number of publications citing work performed using optical biosensor technology compared with the previous year. We collated the 962 total papers for 2003, identified the geographical regions where the work was performed, highlighted the instrument types on which it was carried out, and segregated the papers by biological system. In this overview, we spotlight 13 papers that should be on everyone's 'must read' list for 2003 and provide examples of how to identify and interpret high-quality biosensor data. Although we still find that the literature is replete with poorly performed experiments, over-interpreted results and a general lack of understanding of data analysis, we are optimistic that these shortcomings will be addressed as biosensor technology continues to mature.

https://onlinelibrary.wiley.com/doi/pdf/10.1002/jmr.753

Survey of the year 2003 commercial optical biosensor literature

Most methods for the analysis of oligosaccharides from biological sources require a glycan derivatization step: glycans may be derivatized to introduce a chromophore or fluorophore, facilitating detection after chromatographic or electrophoretic separation. Derivatization can also be applied to link charged or hydrophobic groups at the reducing end to enhance glycan separation and mass-spectrometric detection. Moreover, derivatization steps such as permethylation aim at stabilizing sialic acid residues, enhancing mass-spectrometric sensitivity, and supporting detailed structural characterization by (tandem) mass spectrometry. Finally, many glycan labels serve as a linker for oligosaccharide attachment to surfaces or carrier proteins, thereby allowing interaction studies with carbohydrate-binding proteins. In this review, various aspects of glycan labeling, separation, and detection strategies are discussed.

/pdf/glycan-labeling-strategies-and-their-use-in-identification-sjibhzrtrz.pdf

Glycan labeling strategies and their use in identification and quantification

Post-translational Modifications Differentially Affect IgG1 Conformation and Receptor Binding

A robust, high-throughput assay to determine the phagocytic activity of clinical antibody samples

Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action

Glycoform-dependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy.

We report herein the first mass spectrometric analyses of isotopomers of a pyridylamino (PA)-derivatized biantennary oligosaccharide, in which one of two non-reducing terminal galactose residues is selectively enriched in 13C by an enzymatic reaction. By use of these isotopomeric PA-oligosaccharides, individual fragment ions observed in tandem mass spectra of MALDI-QIT-TOF-MS were unambiguously assigned. It was shown that the oligosaccharide ion that lacks the N-acetyllactosamine previously linked to the Manα1 →6 antenna dominates its isomeric counterpart ion. We propose that tandem mass spectrometric analyses of oligosaccharides isotopically labeled at a selected antenna would provide us with the basis of mechanisms of formation of glycosidic linkage fragment ions.

Mamiko Nishimura

Papers

Glycoform-dependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy.

Discrimination of Isomeric Fragment Ions Observed in Tandem Mass Spectra of Biantennary Oligosaccharides by Use of Selective Isotope Labeling