What is it about?
Unexpected disulfide bonds - or ones different from your expectation - can change the properties of a protein dramatically. This may involve different immunulogical reactions, the proteins function and stability. The goal of this work is to accelerate and automate this kind of analysis and to make the laboratory experiments much simpler.
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Why is it important?
Unexpected disulfide bonds can have significant influence on the speed and likelihood of a new protein drug to be marketed and to be safely used by patients.
Perspectives
I think the article might change the perception of MALDI in peoples mind of how complicated it is. And how useful it actually can be in solving quite complex tasks relatively quickly and which are quite difficult otherwise to tackle by classic electrospray approaches.
Detlev Suckau
Bruker Corporation
This study is a nice example of how MALDI unique ionization and activation properties can help address challenging analytical questions with a relatively simple methodology. The De Novo detection of disulfide linkages and the ability to detect peptides with multiple cross links is a powerful tool for the understanding of proteins higher order structure.
Guillaume Tremintin
Bruker Corporation
Read the Original
This page is a summary of: Rapid, automated characterization of disulfide bond scrambling and IgG2 isoform determination, mAbs, October 2018, Taylor & Francis,
DOI: 10.1080/19420862.2018.1512328.
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