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Abstract Electrical magnetoresistance and tunnel diode oscillator measurements were performed under external magnetic fields up to 41 T applied along the crystallographic b axis (hard axis) of UTe 2 as a function of temperature and applied pressures up to 18.8 kbar. In this work, we track the field-induced first-order transition between superconducting and magnetic field-polarized phases as a function of applied pressure, showing suppression of the transition with increasing pressure until the demise of superconductivity near 16 kbar and the appearance of a pressure-induced ferromagnetic-like ground state that is distinct from the field-polarized phase and stable at zero field. Together with evidence for the evolution of a second superconducting phase and its upper critical field with pressure, we examine the confinement of superconductivity by two orthogonal magnetic phases and the implications for understanding the boundaries of triplet superconductivity. 

Multivalent display of receptor-engaging antibodies or ligands can enhance their activity. Instead of achieving multivalency by attachment to preexisting scaffolds, here we unite form and function by the computational design of nanocages in which one structural component is an antibody or Fc-ligand fusion and the second is a designed antibody-binding homo-oligomer that drives nanocage assembly. Structures of eight nanocages determined by electron microscopy spanning dihedral, tetrahedral, octahedral, and icosahedral architectures with 2, 6, 12, and 30 antibodies per nanocage, respectively, closely match the corresponding computational models. Antibody nanocages targeting cell surface receptors enhance signaling compared with free antibodies or Fc-fusions in death receptor 5 (DR5)–mediated apoptosis, angiopoietin-1 receptor (Tie2)–mediated angiogenesis, CD40 activation, and T cell proliferation. Nanocage assembly also increases severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pseudovirus neutralization by α-SARS-CoV-2 monoclonal antibodies and Fc–angiotensin-converting enzyme 2 (ACE2) fusion proteins.