Recently Designed Multivalent Spike Binders Cannot Bind Multivalently─How Do They Achieve Enhanced Avidity to SARS-CoV-2?
| dc.contributor.author | Erickson, Harold P | |
| dc.contributor.author | Corbin Goodman, Lauren | |
| dc.date.accessioned | 2022-09-04T20:30:42Z | |
| dc.date.available | 2022-09-04T20:30:42Z | |
| dc.date.issued | 2022-08-09 | |
| dc.date.updated | 2022-09-04T20:30:41Z | |
| dc.description.abstract | The trimeric spike protein of SARS-CoV-2 has been targeted by antibody mimics that bind near or at the receptor-binding domain to neutralize the virus. Several independent studies have reported enhanced binding avidity for dimers and trimers, where binding domains are connected by short peptides. The enhanced avidity of the multivalent constructs was attributed to their simultaneously binding two or three sites within a single spike trimer. We argue here that the 15-20 amino acid peptide linkers, when considered as worm-like-chains, are too short to span the binding sites within a single spike. The enhanced avidity of the multivalent constructs may be explained by a rebinding mechanism, which does not involve multivalent binding. | |
| dc.identifier.issn | 0006-2960 | |
| dc.identifier.issn | 1520-4995 | |
| dc.identifier.uri | ||
| dc.language | eng | |
| dc.publisher | American Chemical Society (ACS) | |
| dc.relation.ispartof | Biochemistry | |
| dc.relation.isversionof | 10.1021/acs.biochem.2c00291 | |
| dc.title | Recently Designed Multivalent Spike Binders Cannot Bind Multivalently─How Do They Achieve Enhanced Avidity to SARS-CoV-2? | |
| dc.type | Journal article | |
| duke.contributor.orcid | Erickson, Harold P|0000-0002-9104-8987 | |
| pubs.organisational-group | Duke | |
| pubs.organisational-group | School of Medicine | |
| pubs.organisational-group | Basic Science Departments | |
| pubs.organisational-group | Institutes and Centers | |
| pubs.organisational-group | Cell Biology | |
| pubs.organisational-group | Duke Cancer Institute | |
| pubs.publication-status | Published |