| Autor: |
Dustin Britton, Kamia Punia, Farbod Mahmoudinobar, Takuya Tada, Xunqing Jiang, P. Douglas Renfrew, Richard Bonneau, Nathaniel R. Landau, Xiang-Peng Kong, Jin Kim Montclare |
| Rok vydání: |
2022 |
| Předmět: |
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| Zdroj: |
Biochemical engineering journal. 187 |
| ISSN: |
1369-703X |
| Popis: |
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has caused a global pandemic since December 2019, and with it, a push for innovations in rapid testing and neutralizing antibody treatments in an effort to solve the spread and fatality of the disease. One such solution to both of these prevailing issues is targeting the interaction of SARS-CoV-2 spike receptor binding domain (RBD) with the human angiotensin-converting enzyme 2 (ACE2) receptor protein. Structural studies have shown that the N-terminal alpha-helix comprised of the first 23 residues of ACE2 plays an important role in this interaction. Where it is typical to design a binding domain to fit a target, we have engineered a protein that relies on multivalency rather than the sensitivity of a monomeric ligand to provide avidity to its target by fusing the N-terminal helix of ACE2 to the coiled-coil domain of the cartilage oligomeric matrix protein. The resulting ACE-MAP is able to bind to the SARS-CoV-2 RBD with improved binding affinity, is expressible in |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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Full Text from ScienceDirect