Abstract
Programming protein nanomaterials to respond to changes in environmental conditions is a current challenge for protein design and is important for targeted delivery of biologics. Here we describe the design of octahedral non-porous nanoparticles with a targeting antibody on the two-fold symmetry axis, a designed trimer programmed to disassemble below a tunable pH transition point on the three-fold axis, and a designed tetramer on the four-fold symmetry axis. Designed non-covalent interfaces guide cooperative nanoparticle assembly from independently purified components, and a cryo-EM density map closely matches the computational design model. The designed nanoparticles can package protein and nucleic acid payloads, are endocytosed following antibody-mediated targeting of cell surface receptors, and undergo tunable pH-dependent disassembly at pH values ranging between 5.9 and 6.7. The ability to incorporate almost any antibody into a non-porous pH-dependent nanoparticle opens up new routes to antibody-directed targeted delivery.
Cite
CITATION STYLE
Yang, E. C., Divine, R., Miranda, M. C., Borst, A. J., Sheffler, W., Zhang, J. Z., … Baker, D. (2024). Computational design of non-porous pH-responsive antibody nanoparticles. Nature Structural and Molecular Biology, 31(9), 1404–1412. https://doi.org/10.1038/s41594-024-01288-5
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