Articles in the Category ”References”

FabALACTICA® in a Quantitative IgG1 Clone Profiling

September 23, 2021 | Applications, References |

Our immune system protects us from pathogens and various diseases, and the immune response is dependent on a person’s repertoire of immune cells, antibodies and circulating plasma proteins. A detailed characterization of these plasma components is important for the understanding of how they affect each individual’s immune response.
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FabRICATOR® in a DAR Analysis of Antibody-Oligonucleotide Conjugates

September 16, 2021 | Applications, References |

In this paper, scientists at Spectroswiss and Orion Pharma present a novel strategy for DAR analysis of structurally complex antibody-oligonucleotide conjugates using SmartEnzymes™ and a proteoform integration approach combined with native SEC-Orbitrap FTMS.
 
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FabRICATOR in a Comprehensive Characterization of a Bispecific Antibody

September 9, 2021 | Applications, References |

Scientists at University of Geneva and Centre d’Immunologie Pierre-Fabre here describes a comprehensive intact and middle-level characterization of a commercial bispecific antibody by using a variety of orthogonal chromatographic methods coupled to MS.
 
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GingisREX® in a Bottom-Up Analysis of Histones


Bottom-up mass spectrometry where the intact protein is digested into smaller peptides is an indispensable tool for proteomics and the studying of histone codes. Since histones are enriched with the basic amino acids arginine and lysine, enzymatic digestion is often challenging as peptides too short for LC retention and PTM localization are generated. In addition, the complex workflow entails that the combination of samples preparation, data acquisition and analysis provides a different image of the histone code.

 

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Purification of Antibody Fragments via Hydrophobic Interactions


The importance of monoclonal antibodies (mAbs) as therapeutic agents is steadily increasing, and each year nearly 300 novel mAbs are being evaluated for their therapeutic effectivity. Interest has also been expressed in the use of antibody fragments as therapeutic agents. The physiochemical properties of the fragments differ significantly from that of intact antibodies, and the fragments can more easily be coupled to dyes, toxins and vesicles for diagnostic purposes, cancer therapy and improved drug delivery, respectively.
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Analytical Methods to Monitor Site-Specific ADC Generation with GlyCLICK®


Scientists at the University of Strasbourg and University of Geneva use innovative native MS and IM methodologies for analytical characterization of a site-specific ADC generated with the GlyCLICK technology.

 

Antibody-drug conjugates (ADCs) combine the benefits of tumor-targeting monoclonal antibodies with the cytotoxic effect of drug payloads covalently linked to the antibody. The ADC generation process has evolved from non-selective and uncontrolled conjugation in early generation products, to site-specific conjugation resulting in homogenous and well-defined ADCs. Conjugation at the antibody Fc glycan sites using the GlyCLICK technology has proven to be an attractive option for the generation of site-specific ADCs.
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Middle-up Analysis of Monoclonal Antibodies using FabRICATOR®


With their molecular specificity for biological targets, monoclonal antibodies (mAbs) have revolutionized the field of research and medicine. Due to numerous post-translational modifications causing heterogeneity in the structure of mAbs, a comprehensive characterization of the physiochemical properties is necessary to ensure the quality, efficacy and safety of mAb-based therapeutic drugs.
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FabALACTICA Facilitates the Structural Insight into SARS-CoV-2 Neutralizing Antibodies


The first steps of infection with SARS-CoV-2 is binding of a viral Spike protein to a host receptor angiotensin-converting enzyme 2 (ACE2), followed by fusion of viral and host membranes. Antibodies that block this interaction are emerging as early COVID-19 therapies, however, the neutralization potencies of the antibodies are less studied.
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Characterization of SARS-CoV-2 Receptor-Binding Domains using SmartEnzymes™


Scientists at Leiden University Medical Center (LUMC) present a multilevel mass spectrometry approach using SmartEnzymes for in-depth characterization of mammalian SARS-CoV-2 receptor-binding (RBD) domains.

 

The COVID-19 disease caused by the SARS-CoV-2 virus has affected more that 100 million individuals in the ongoing pandemic. The enveloped RNA corona virus contains three structural proteins in the membrane, including the heavily glycosylated spike protein carrying 22 N-glycosylation sites. The spike protein in turn consists of two subunits, S1 and S2, where the receptor-binding domain (RBD) of S1 directly interacts with the ACE2 receptor in the human respiratory tract and facilitates host cell entry. Considering the relevance of RBD glycosylation on ACE2 binding and recognition by neutralizing antibodies, the use of well-characterized S proteins is essential for continued research and development of diagnostic tools and vaccines.

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FabRICATOR in an Evaluation of Mobile-phase Additives for LC-MS Characterization of mAbs


Biopharmaceuticals, including monoclonal antibodies (mAbs), have become an important class of therapeutics. The manufacturing procedure of mAbs is complex, and many possible variants of a particular mAb can be generated as a result of enzymatical and chemical modifications. Some of these modifications are critical for the efficacy and safety of the therapeutic mAb and are known as critical quality attributes (CQAs). CQAs need to be thoroughly monitored to ensure the quality and safety of the therapeutic agent.

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