AbstractsBiology & Animal Science

Analysis of crystal structures of native antibodies bound to the hemagglutinin (HA) surface receptor of influenza have provided pertinent chemical information and metrics of the antibody-antigen interactions at the complimentary determining region (CDR) and receptor-binding domain (RBD) interface. We proposed that using this information, we could design a gold monolayer-protected cluster (AuMPC) functionalized with peptidic anti-HA paratopes and determine equilibrium rate constants of this particle-protein interaction. The peptidic ligands incorporate thiol surface modulators, polyethylene glycol spacing module, and specificity through a molecular recognition element (MRE). The MRE will be based upon the amino acid sequences of CDRs of specific antibodies to HA of pandemic influenza virus. Bio-layer interferometry experiments were conducted with these AuMPCs to determine equilibrium rate constants. The modular design of our ligands coupled with our platform made for an interdisciplinary and novel approach to nanoparticle biomimetics.