期刊
PROTEOMICS
卷 21, 期 21-22, 页码 -出版社
WILEY
DOI: 10.1002/pmic.202000300
关键词
antibody antigen interactions; antibody deign; native mass spectrometry; protein stability
资金
- National Institutes of Health/National Institute of General Medical Sciences
- Israel Science Foundation [300/17]
- Clore Israel Foundation
The study utilized direct-mass spectrometry approach for rapid structural characterization of designed antibodies directly from crude growth media, without the need for prior purification. This method allows for defining properties such as stability, specificity and interactions with antigens.
In recent decades, antibodies (Abs) have attracted the attention of academia and the biopharmaceutical industry due to their therapeutic properties and versatility in binding a vast spectrum of antigens. Different engineering strategies have been developed for optimizing Ab specificity, efficacy, affinity, stability and production, enabling systematic screening and analysis procedures for selecting lead candidates. This quality assessment is critical but usually demands time-consuming and labor-intensive purification procedures. Here, we harnessed the direct-mass spectrometry (direct-MS) approach, in which the analysis is carried out directly from the crude growth media, for the rapid, structural characterization of designed Abs. We demonstrate that properties such as stability, specificity and interactions with antigens can be defined, without the need for prior purification.
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