Three dimensional (3D) supramolecules with giant cavities are attractive due to their wide range of applications. Herein, we used pentatopic terpyridine ligands with three types of coordination moieties to assemble two giant supramolecular hexagonal prisms with a molecular weight up to 42 608 and 43 569 Da, respectively. Within the prisms, two double-rimmed Kandinsky Circles serve as the base surfaces as well as the templates for assisting the self-sorting during the self-assembly. Additionally, hierarchical self-assembly of these supramolecular prisms into tubular-like nanostructures was fully studied by scanning tunneling microscopy (STM) and small-angle X-ray scattering (SAXS). Finally, these supramolecular prisms show good antimicrobial activities against Gram-positive pathogen methicillin-resistant Staphylococcus aureus (MRSA) and Bacillus subtilis (B. subtilis).

Coordination-driven self-assembly as a bottom-up approach has witnessed a rapid growth in building giant structures in the past few decades. Challenges still remain, however, within the construction of giant architectures in terms of high efficiency and complexity from simple building blocks. Inspired by the features of DNA and protein, which both have specific sequences, we herein design a series of linear building blocks with specific sequences through the coordination between terpyridine ligands and Ru(II). Different generations of polycyclic supramolecules (C1 to C5) with increasing complexity are obtained through the self-assembly with Cd(II), Fe(II) or Zn(II). The assembled structures are characterized via multi-dimensional mass spectrometry analysis as well as multi-dimensional and multinuclear NMR (1H, COSY, NOESY) analysis. Moreover, the largest two cycles C4 and C5 hierarchically assemble into ordered nanoscale structures on a graphite based on their precisely-controlled shapes and sizes with high shape-persistence.

In this study,w ee stablished af easible strategy to construct an ew type of metallo-polymer with helicoidal structure through the combination of covalent polymerization and intramolecular coordination-driven self-assembly.I nt he design, at etratopic monomer (M)w as prepared with two terminal alkynes in the outer rim for polymerization, and two terpyridines (TPYs) in the inner rim for subsequent folding by selective intramolecular coordination. Then, the linear covalent polymer (P)w as synthesized by polymerization of M via Glaser-Hay homocoupling reaction. Finally,i ntramolecular coordination interactions between TPYs and Zn(II) folded the backbone of P into aright-or left-handed metallo-helicoid (H) with double rims.O wing to multiple positive charges on the inner rim of helicoid, double-stranded DNAm olecules (dsDNA) could interact with H through electrostatic interactions.R emarkably,d sDNAa llowed exclusive formation of H with right handedness by means of chiral induction. Figure 1. Cartoon representation of helix (left) and helicoid (right).

In this study,w ee stablished af easible strategy to construct an ew type of metallo-polymer with helicoidal structure through the combination of covalent polymerization and intramolecular coordination-driven self-assembly.I nt he design, at etratopic monomer (M)w as prepared with two terminal alkynes in the outer rim for polymerization, and two terpyridines (TPYs) in the inner rim for subsequent folding by selective intramolecular coordination. Then, the linear covalent polymer (P)w as synthesized by polymerization of M via Glaser-Hay homocoupling reaction. Finally,i ntramolecular coordination interactions between TPYs and Zn(II) folded the backbone of P into aright-or left-handed metallo-helicoid (H) with double rims.O wing to multiple positive charges on the inner rim of helicoid, double-stranded DNAm olecules (dsDNA) could interact with H through electrostatic interactions.R emarkably,d sDNAa llowed exclusive formation of H with right handedness by means of chiral induction. Figure 1. Cartoon representation of helix (left) and helicoid (right).

The aggregation of the prion protein (PrP) plays a key role in the development of prion diseases and is believed to be an autocatalytic process with a very high kinetic barrier. Intensive studies have focused on overcoming the kinetic barriers under extremely nonphysiological in vitro conditions by altering the pH of PrP solution on solid surfaces, such as gold, mica, and a lipid bilayer. Importantly, sulfated glycosaminoglycans (GAGs), including heparin, were found to be associated with PrP misfolding and aggregation, suggesting GAGs have catalytic roles in PrP aggregation processes. However, the exact role and details of GAGs in the PrP aggregation are not clear and need a thorough perusal. Here, we investigate the PrP aggregation process on a heparin functionalized gold surface by in situ, real-time monitoring of the atomic scale details of the whole aggregation process by single molecule atomic force microscopy (AFM), combining simultaneous topographic and recognition (TREC) imaging and single molecule force spectroscopy (SMFS). We observed the whole aggregation process for full-length human recombinant PrP (23−231) aggregation on the heparin modified gold surface, from the formation of oligomers, to the assembly of protofibrils and short fibers, and the formation of elongated mature fibers. Heparin is found to promote the PrP aggregation by facilitating the formation of oligomers during the early nucleation stage.