Summary
Conformational entropy of loops of antibodies is inversely proportional to antigen-binding affinity (1–2).
Figures
Ref (1)
1.
Mikolajek H, Weckener M, Brotzakis ZF, Huo J, Dalietou EV, Le Bas A, et al. Correlation between the binding affinity and the conformational entropy of nanobody SARS-CoV-2 spike protein complexes. Proceedings of the National Academy of Sciences. 2022;119(31). Available from: https://doi.org/10.1073/pnas.2205412119
2.
Thorpe IF, Brooks CL. Molecular evolution of affinity and flexibility in the immune system. Proceedings of the National Academy of Sciences. 2007;104(21):8821–6. Available from: https://doi.org/10.1073/pnas.0610064104
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Löhr T, Sormanni P, Vendruscolo M. Conformational Entropy as a Potential Liability of Computationally Designed Antibodies. Biomolecules. 2022;12(5):718. Available from: https://doi.org/10.3390/biom12050718