Synthesis of proteins by automated flow chemistry
| Autor: | Nina Hartrampf, Shunying Liu, Carly K. Schissel, Sarah Antilla, Alexander J. Mijalis, Thomas E. Nielsen, Zachary P. Gates, Amanda E. Cowfer, Andrei Loas, Azin Saebi, Alex J. Callahan, Anthony J. Quartararo, Stephanie Hanna, Mark D. Simon, Mackenzie Poskus, Carsten Jessen, Xiyun Ye, Bradley L. Pentelute |
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| Přispěvatelé: | Massachusetts Institute of Technology. Department of Chemistry |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
chemistry.chemical_classification
Protein Folding Multidisciplinary 010405 organic chemistry Chemistry Protein domain Proteins Peptide Flow chemistry 010402 general chemistry 01 natural sciences Ribosome Chemical synthesis 0104 chemical sciences Amino acid Folding (chemistry) chemistry.chemical_compound Protein Domains Biochemistry Peptide synthesis Protein biosynthesis Protein folding Peptides Solid-Phase Synthesis Techniques |
| Zdroj: | chemRxiv |
| Popis: | Ribosomes can produce proteins in minutes and are largely constrained to proteinogenic amino acids. Here, we report highly efficient chemistry matched with an automated fast-flow instrument for the direct manufacturing of peptide chains up to 164 amino acids long over 327 consecutive reactions. The machine is rapid: Peptide chain elongation is complete in hours. We demonstrate the utility of this approach by the chemical synthesis of nine different protein chains that represent enzymes, structural units, and regulatory factors. After purification and folding, the synthetic materials display biophysical and enzymatic properties comparable to the biologically expressed proteins. High-fidelity automated flow chemistry is an alternative for producing single-domain proteins without the ribosome. National Science Foundation (Grant 1122374) |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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