The advent of additive manufacturing has facilitated the design and fabrication of hybrid lattice structures with multiple morphologies. These structures combine multiple distinct architectures into a single structure with an exceptional performance that far exceeds that of each constituting architecture. However, combining strut-based lattices poses serious challenges in establishing effective connections, primarily due to complications in formulating mathematical expressions. Here, we introduce a novel approach, inspired by the connections observed in the grain boundaries of polycrystalline materials, to design the interconnections of hybrid structures. This strategy involves shrinking the unit cell linkage, thereby addressing the difficulty of forming efficient connections at arbitrary spatial interfaces within strut-based lattice structures. We then use the relevant design theories to tune the performance of these connections and simplify the design process for hybrid structures – even for inexperienced designers. Our experimental observations confirm the efficacy of the proposed strategy, bridging the knowledge gap in the design of connected strut-based multi-lattice structures. Furthermore, this approach enhances the design of tailored hybrid structures and fosters the development of metamaterials with advanced, unique functionalities. The proposed approach has important implications for the development of designer materials, with applications in medical devices, (soft) robotics, and implants.

The chaperone heat shock protein 90 (Hsp90) is well known to undergo important conformational changes, which depend on nucleotide and substrate interactions. Conversely, how the conformations of its unstable and disordered substrates are affected by Hsp90 is difficult to address experimentally yet is central to its function. Here, using optical tweezers, we find that Hsp90 promotes local contractions in unfolded chains that drive their global compaction down to dimensions of folded states. This compaction has a gradual nature while showing small steps, is stimulated by ATP, and performs mechanical work against counteracting forces that expand the chain dimensions. The Hsp90 interactions suppress the formation of larger-scale folded, misfolded, and aggregated structures. The observations support a model in which Hsp90 alters client conformations directly by promoting local intra-chain interactions while suppressing distant ones. We conjecture that chain compaction may be central to how Hsp90 protects unstable clients and cooperates with Hsp70.