Robust and high affinity recombinant antibodies have become a cornerstone of therapeutic drug development. However, for infectious inhibitory antibodies it is required that they bind with extraordinary affinity or be administered at high dosage, to ensure full neutralization of the infectious agent. Often loss of binding strength is observed when mutant vira occur. The objective is to develop a novel therapeutic concept where recombinant antibodies are fused to dimerization domains. The dimerization domains interact specifically with low to medium affinity; an affinity insufficient to mediate multimerization in serum. When antibodies recognize their targets on the surface of SARS-CoV-2, the local concentration of antibodies increases, thereby facilitating dimerization interaction. The resulting avidity effect will lead to more antibodies recruited to the infectious agent. By targeting multiple epitope on the viral membrane protein, loss of effect due to mutations should be minimized.
|Effektiv start/slut dato||01/10/2022 → 30/09/2025|
Udforsk forskningsemnerne, som dette projekt berører. Disse etiketter er oprettet på grundlag af de underliggende bevillinger/legater. Sammen danner de et unikt fingerprint.