Selected article for: "binding affinity and domain protein"

Author: Czajka, Timothy F.; Vance, David J.; Mantis, Nicholas J.
Title: Slaying SARS-CoV-2 One (Single-Domain) Antibody at a Time
  • Cord-id: jdq859xc
  • Document date: 2020_12_16
  • ID: jdq859xc
    Snippet: Camelid-derived and synthetic single-domain antibodies (sdAbs) are emerging as potent weapons against the novel coronavirus, SARS-CoV-2. SdAbs are small, compact, thermostable immunoglobulin elements capable of binding targets with sub-nanomolar affinities. By leveraging the power of phage- and yeast surface-display technologies, rare sdAbs can be isolated from highly diverse and complex antibody libraries. Once in hand, sdAbs can be engineered to improve binding affinity, avidity, target specif
    Document: Camelid-derived and synthetic single-domain antibodies (sdAbs) are emerging as potent weapons against the novel coronavirus, SARS-CoV-2. SdAbs are small, compact, thermostable immunoglobulin elements capable of binding targets with sub-nanomolar affinities. By leveraging the power of phage- and yeast surface-display technologies, rare sdAbs can be isolated from highly diverse and complex antibody libraries. Once in hand, sdAbs can be engineered to improve binding affinity, avidity, target specificities, and bio-distribution. In this Opinion piece, we highlight a series of sophisticated studies describing the identification of ultrapotent sdAbs directed against the receptor binding domain (RBD) of the SARS-CoV-2 Spike protein. We discuss the possible applications of these antibodies in the global fight against COVID-19.

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