A comparison of the binding sites of antibodies and single-domain antibodies

Antibodies are the largest class of biotherapeutics. However, in recent years, single-domain antibodies have gained traction due to their smaller size and comparable binding affinity. (Abs) (sdAbs) differ structures sites: most significantly, lack a light chain so just three CDR loops. Given this inherent structural difference, it is important understand whether Abs sdAbs distinguishable how they engage partner thus, suited different types epitopes. In study, we use non-redundant sequence datasets compare paratopes, epitopes antigen interactions sdAbs. We demonstrate that even though target equal those targeted by Abs. To achieve this, paratopes contribute more per residue than Additionally, find conserved framework residues increased importance sdAbs, suggesting include non-specific Furthermore, only marginally less accessible Abs: posit may be explained differences orientation compaction sdAb Ab CDR-H3 Overall, our results implications for engineering humanization as well selection best modality targeting particular epitope.