Semisynthesis of Human Ribonuclease-S
| Autor: | Ronald T. Raines, Evans C. Wralstad, Jessica Sayers |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
RNase P
Biomedical Engineering Pharmaceutical Science Bioengineering Bovine pancreatic ribonuclease Cleavage (embryo) Article Ribonucleases Peptide bond Humans Ribonuclease Amino Acid Sequence Pharmacology chemistry.chemical_classification biology Organic Chemistry Ribonuclease Pancreatic Semisynthesis Enzyme chemistry Biochemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein Pancreatic ribonuclease Electrophoresis Polyacrylamide Gel Biotechnology |
| Zdroj: | Bioconjug Chem |
| ISSN: | 1520-4812 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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