Bamlanivimab

Bamlanivimab (300 nM; 5 min association, 15 min dissociation) exhibits high-affinity binding to the soluble trimeric SARS-CoV-2 spike protein, with an apparent K_d within a 100-fold range of other RBD-binding antibodies tested^[1].

Bamlanivimab (20 nM SARS-CoV-2 spike protein, 200 nM ACE2; 12 h pre-incubation, 5 min association, 1 min dissociation) competes with human ACE2 for binding to the SARS-CoV-2 spike protein^[1].
Bamlanivimab (0.01-10 μg/mL; 45 min pre-incubation with virus, 72 h incubation with cells) potently neutralizes SARS-CoV-2 spike pseudotyped lentivirus in ACE2-transfected 293T cells^[1].
Bamlanivimab (0.001-1000 μg/mL; 1 h pre-incubation with virus, 48 h incubation with cells) potently neutralizes a replication-competent luciferase reporter SARS-CoV-2 in Vero E6 cells^[1].
Bamlanivimab (0.001-100 μg/mL; 1-2 h pre-incubation with virus, 48 h (INMI-1) or 72 h (USA/WA-1) incubation with cells) potently neutralizes two clinical SARS-CoV-2 isolates (INMI-1 and USA/WA-1/2020) in Vero E6 cells via plaque reduction^[1].
Bamlanivimab (~12 mg/mL Fab-RBD complex; crystallization occurred within 1-2 days, harvested on day 3) binds to an ACE2-overlapping epitope on the SARS-CoV-2 RBD, with specific atomic interactions that block ACE2 engagement^[1].
Bamlanivimab binds to the SARS-CoV-2 spike protein RBD in both the up and down conformations, allowing recognition of the spike in multiple states of viral entry^[1].

Bamlanivimab induces antibody-dependent cell-mediated cytotoxicity in vitro using spike protein-expressing target cells and reporter cells, supporting enhanced viral clearance via intrinsic immune activation^[2].