Journal
BIOCONJUGATE CHEMISTRY
Volume 32, Issue 1, Pages 82-87Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.bioconjchem.0c00557
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Funding
- Graduate Research Fellowship from the NSF
- NIH [R01 CA073808]
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The ribonuclease S complex has led to historic discoveries in protein chemistry and enzymology, but its applications have been hindered by two main drawbacks: immune response in humans and susceptibility to dissociation. By semi-synthesizing an RNase S conjugate derived from human pancreatic ribonuclease and stabilized with a covalent interfragment cross-link, these limitations have been addressed, enabling unprecedented applications of the RNase-S system.
Since its conception, the ribonuclease S complex (RNase S) has led to historic discoveries in protein chemistry, enzymology, and related fields. Derived by the proteolytic cleavage of a single peptide bond in bovine pancreatic ribonuclease (RNase A), RNase S serves as a convenient and reliable model system for incorporating unlimited functionality into an enzyme. Applications of the RNase S system in biomedicine and biotechnology have, however, been hindered by two shortcomings: (1) the bovine-derived enzyme could elicit an immune response in humans, and (2) the complex is susceptible to dissociation. Here, we have addressed both limitations in the first semisynthesis of an RNase S conjugate derived from human pancreatic ribonuclease and stabilized by a covalent interfragment cross-link. We anticipate that this strategy will enable unprecedented applications of the RNase-S system.
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