High affinity interaction between S-protein and S-peptide fragments of bovine pancreatic RNase A has been recently used for construction of molecular vehicles for targeted drug delivery. The vehicle is assembled as a complex of drug carrier conjugated S-protein with S-peptide-tagged targeting protein. To avoid random chemical crosslinking of drug carriers to S-protein, we constructed a mutant 16-124aa fragment of RNase A in which 122ala is replaced with a cysteine residue. The mutant and the corresponding wild type fragments expressed in Escherichia coli are refolded into functional conformations only in the presence of S-peptide. After the removal of S-peptide, both fragments retain the ability to bind S-peptide and S-peptide-tagged proteins. The 122cys residue in the mutant fragment is available for site-specific conjugation. © 2002 Elsevier Science (USA). All rights reserved.
CITATION STYLE
Backer, M. V., Gaynutdinov, T. I., Aloise, R., Przekop, K., & Backer, J. M. (2002). Engineering S-protein fragments of bovine ribonuclease A for targeted drug delivery. Protein Expression and Purification, 26(3), 455–461. https://doi.org/10.1016/S1046-5928(02)00546-6
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