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Semisynthesis of Human Ribonuclease–S
Name
nihms-1654238.pdf
Description
Accepted version
Size
993.98 KB
Format
Adobe PDF
Checksum (MD5)
8a354b7e223c475e2f7d7ed6f95ee587
Author(s)
Sayers, Jessica
Wralstad, Evans C
Raines, Ronald T
Date Issued
2021
Journal
Bioconjugate Chemistry
Publisher
American Chemical Society (ACS)
Citation
Sayers, Jessica, Wralstad, Evans C and Raines, Ronald T. 2021. "Semisynthesis of Human Ribonuclease–S." Bioconjugate Chemistry, 32 (1).
Version
Author's final manuscript
Abstract
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.
Terms of Use
Creative Commons Attribution-Noncommercial-Share Alike
Persistent DSpace Link
DOI of Published Version
10.1021/ACS.BIOCONJCHEM.0C00557
