No barriers to growing a row: Classical nucleation theory predicts that two-dimensional islands on a surface must reach a critical size before they continue to grow; below that size, they dissolve. Chen et al. used phage display to select for short peptides that would bind to molybdenum disulfide (MoS ₂ ) (see the Perspective by Kahr and Ward). Hexagonal arrays of these peptides grew epitaxially as dimers but without a size barrier—the critical nuclei size was zero. Although two-dimensional arrays formed, growth occurred one row at time. Classical nucleation theory indeed predicts the absence of a barrier for such one-dimensional growth. Science , this issue p. 1135 ; see also p. 1111

The functionalized lipid shell of hybrid nanoparticles plays an important role for improving their biocompatibility and in vivo stability. Yet few efforts have been made to critically examine the shell structure of nanoparticles and its effect on cell–particle interaction. Here we develop a microfluidic chip allowing for the synthesis of structurally well-defined lipid-polymer nanoparticles of the same sizes, but covered with either lipid-monolayer-shell (MPs, monolayer nanoparticles) or lipid-bilayer-shell (BPs, bilayer nanoparticles). Atomic force microscope and atomistic simulations reveal that MPs have a lower flexibility than BPs, resulting in a more efficient cellular uptake and thus anticancer effect than BPs do. This flexibility-regulated cell–particle interaction may have important implications for designing drug nanocarriers.

Layered double hydroxides (LDHs), also well-known as hydrotalcite-like layered clays, have been widely investigated in the fields of catalysts and catalyst support, anion exchanger, electrical and optical functional materials, flame retardants and nanoadditives. This feature article focuses on the progress in micro-/nanostructured LDHs in terms of morphology, and also on the preparations, applications, and perspectives of the LDHs with different morphologies.

Uncontrolled misfolding of proteins leading to the formation of amyloid deposits is associated with more than 40 types of diseases, such as neurodegenerative diseases and type-2 diabetes. These irreversible amyloid fibrils typically assemble in distinct stages. Transitions among the various intermediate stages are the subject of many studies but are not yet fully elucidated. Here, we combine high-resolution atomic force microscopy and quantitative nanomechanical mapping to determine the self-assembled structures of the decapeptide hIAPP _20–29 , which is considered to be the fibrillating core fragment of the human islet amyloid polypeptide (hIAPP) involved in type-2 diabetes. We successfully follow the evolution of hIAPP _20–29 nanostructures over time, calculate the average thickening speed of small ribbon-like structures, and provide evidence of the coexistence of ribbon and helical fibrils, highlighting a key step within the self-assembly model. In addition, the mutations of individual side chains of wide-type hIAPP _20–29 shift this balance and destabilize the helical fibrils sufficiently relative to the twisted ribbons to lead to their complete elimination. We combine atomic force microscopy structures, mechanical properties, and solid-state NMR structural information to build a molecular model containing β sheets in cross-β motifs as the basis of self-assembled amyloids.