Thermal analysis of protein stability and ligand binding in complex media
نویسندگان
چکیده
• Differential Scanning Calorimetry analysis of complex media mixtures. Novel method for evaluating thermodynamic stability proteins in unpurified solutions. Protein structural effects purification on expressed proteins. ACE2-ACE2 inhibitor interactions analyzed media. Analysis SARS-CoV-2 RBD binding to ACE2 Screening ligands that can bind biologic products vitro expression systems typically requires some the target. Such is often laborious and time consuming as well a limiting challenge. What required, representing an enormous advantage, ability screen crude lysate stage without purification. For purpose, we explore here, utility differential scanning calorimetry (DSC) measurements detecting presence specific their with where they were prepared, i.e. lysates. Model designed mimic analogous conditions comparable those may be encountered actual systems. Results are reported several examples DSC distinctly showed differences thermal denaturation behaviors alone, plus added lysate. obtained Streptavidin/Biotin E. coli lysate, Angiotensin Converting Enzyme 2 (ACE2) by captopril or lisinopril supernatant derived from cultured Human Kidney cells (HEK293). receptor domain (RBD) was also examined. Binding similar consistent inhibitory activity lisinopril.
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ژورنال
عنوان ژورنال: Thermochimica Acta
سال: 2022
ISSN: ['1872-762X', '0040-6031']
DOI: https://doi.org/10.1016/j.tca.2022.179274