Semisynthesis of Human Ribonuclease–S
Name
nihms-1654238.pdf
Description
Accepted version
Size
993.98 KB
Format
Unknown
Checksum (MD5)
8a354b7e223c475e2f7d7ed6f95ee587
Author(s)
Sayers, Jessica
Wralstad, Evans C.
Raines, Ronald T.
Date Issued
December 2020
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.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution-Noncommercial-Share Alike
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DOI of Published Version
https://doi.org/10.1021/acs.bioconjchem.0c00557
