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- W2371188049 abstract "The ultimate goal in protein design is the creation of proteins with desired functions. We have constructed a set of engineered glutathione S-transferases (GST) proteins (denoted GSHKTs) in which peptide fragments (of varying lengths from 8 to 16 amino acids), derived from human high molecular weight kininogen (HK) domain 5, have been inserted into a surface GST loop (between GST residues Gly49 and Leu50). Functionally, these hybrid proteins cause inhibition of endothelial cell proliferation in contrast to the ancestor GST molecule, which does not. Thus, chimeric GSHKTs can potentially be used as therapeutic agents. For a chimeric protein to be used as a therapeutic agent, high stability and retention of biological activity through purification and storage steps is required. However, as the length of the loop increases, the stability of the protein usually decreases. Therefore, we have measured the stability of the GSHKT proteins using differential scanning calorimetry (DSC). DSC analyses have shown that all of the chimeric GSHKT proteins (independently of the size of the inserted peptide) possess roughly 8°C lower stability in comparison with the ancestor GST. According to the loop entropy model, loop closure in proteins becomes entropically more costly as the length of the loop increases. For short fragments, no direct relationship between the length of the inserted peptide and the destabilizing effect has been observed. Inserting the first two residues destabilizes more per residue than the insertion of subsequent longer fragments." @default.
- W2371188049 created "2016-06-24" @default.
- W2371188049 creator A5042586603 @default.
- W2371188049 date "2013-01-01" @default.
- W2371188049 modified "2023-09-27" @default.
- W2371188049 title "Chimeric Glutathione S-Transferases: Properties and Thermodynamic Stability" @default.
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