Evidence for an imidazoline by-product from glycans using tandem mass spectrometry

Duff, R. Joel; Smith, Elaine; Li, Wenzhou; Fodor, Szilan

doi:10.1016/j.chroma.2017.04.036

Cited by 2 publications

(2 citation statements)

References 16 publications

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“…Data acquisition was controlled by Xcalibur™ software (Thermo Fisher Scientific, Waltham, Massachusetts). This method has been described in an earlier paper, see Reference (12).…”

Section: Peptide Mapping Methodsmentioning

confidence: 99%

Fc glycan sialylation of biotherapeutic monoclonal antibodies has limited impact on antibody‐dependent cellular cytotoxicity

et al. 2021

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It has been well-documented that the terminal sugars of Fc glycans can play a critical role in the safety and efficacy of therapeutic monoclonal antibodies (mAbs). However, many of the effects of highly heterogeneous Fc glycan structures have yet to be fully characterized. Different glycosylation patterns can affect Fcdependent activities such as the ability of mAbs to bind Fcγ receptors (FcγRs) on the effector cell surface, which is critical to immune effector functions such as antibody dependent cellular cytotoxicity (ADCC).Previous studies on the impact of sialic acid in the Fc glycan on ADCC has not resulted in consistent conclusions. In our study we tested sialic acid enriched species from a chimeric murine/human kappa light chain IgG1 (mAb1) with known FcγRIIIa binding and ADCC activities. These enriched species contained up to a four-fold increase in sialic acid-containing glycans relative to the typical levels present in therapeutic mAbs, along with other attributes such as oxidized and deamidated species. The ADCC analysis of sialylated

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“…Data acquisition was controlled by Xcalibur™ software (Thermo Fisher Scientific, Waltham, Massachusetts). This method has been described in an earlier paper, see Reference (12).…”

Section: Peptide Mapping Methodsmentioning

confidence: 99%

Fc glycan sialylation of biotherapeutic monoclonal antibodies has limited impact on antibody‐dependent cellular cytotoxicity

et al. 2021

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“…Recent studies on the use of 2-PB on reductive amination reactions for the analytical methods [34,35], organic synthesis [33,44], and protein modification [36], provided an excellent state-of-the-art to develop its new applications. 2-PB is commonly used in organic media [45], or heterogeneous media with a low percentage of water [46]. There are also some examples with a high percentage of water [33,36].…”

Section: Reduction Of the Immobilized Enzymes With 2-picoline Boranementioning

confidence: 99%

Stabilization of Enzymes by Multipoint Covalent Attachment on Aldehyde-Supports: 2-Picoline Borane as an Alternative Reducing Agent

et al. 2018

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Enzyme immobilization by multipoint covalent attachment on supports activated with aliphatic aldehyde groups (e.g., glyoxyl agarose) has proven to be an excellent immobilization technique for enzyme stabilization. Borohydride reduction of immobilized enzymes is necessary to convert enzyme–support linkages into stable secondary amino groups and to convert the remaining aldehyde groups on the support into hydroxy groups. However, the use of borohydride can adversely affect the structure–activity of some immobilized enzymes. For this reason, 2-picoline borane is proposed here as an alternative milder reducing agent, especially, for those enzymes sensitive to borohydride reduction. The immobilization-stabilization parameters of five enzymes from different sources and nature (from monomeric to multimeric enzymes) were compared with those obtained by conventional methodology. The most interesting results were obtained for bacterial (R)-mandelate dehydrogenase (ManDH). Immobilized ManDH reduced with borohydride almost completely lost its catalytic activity (1.5% of expressed activity). In contrast, using 2-picoline borane and blocking the remaining aldehyde groups on the support with glycine allowed for a conjugate with a significant activity of 19.5%. This improved biocatalyst was 357-fold more stable than the soluble enzyme at 50 °C and pH 7. The results show that this alternative methodology can lead to more stable and active biocatalysts.

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Evidence for an imidazoline by-product from glycans using tandem mass spectrometry

Cited by 2 publications

References 16 publications

Fc glycan sialylation of biotherapeutic monoclonal antibodies has limited impact on antibody‐dependent cellular cytotoxicity

Fc glycan sialylation of biotherapeutic monoclonal antibodies has limited impact on antibody‐dependent cellular cytotoxicity

Stabilization of Enzymes by Multipoint Covalent Attachment on Aldehyde-Supports: 2-Picoline Borane as an Alternative Reducing Agent

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