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Double Twisted Photonic Honeycomb Frameworks with Mesoporous Structures
摘要： In nature, materials such as shell, bone, silk, and wood are assembled with hierarchical structures that span lengths from nanometers to centimeters. These biological materials are fascinating targets for replication and mimicry, often owing to their remarkable properties. The intricate and periodic structure of the snow crab (Chionoecetes opilio) exoskeleton that renders it iridescent is described here. It is discovered that the snow crab has a double twisted photonic honeycomb structure constructed by left-handed rotation of chitin nanofibrils around cavities throughout its shell. This new chiral framework provides a foundation for exploring chiral photonics and materials. With the goal of mimicking this intricate network, the iridescent mineralized chitin shell is successfully transferred to calcite, carbon, apatite, and fluorapatite/chitin materials with structural replication. It is shown that the sophisticated organization of the iridescent crab shell leads these new materials to have a distinctive macroscopic combination of multilevel chirality, honeycomb channels, and mesoporosity. These solid-state transformations of snow crab exoskeletons will open the path to making complex hierarchical frameworks of functional porous materials through bioinspired templating.
关键词： honeycomb,coloration,biomimicry,chirality,structural order
更新于2025-09-23 15:23:52
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Probing Specificity of Protein–Protein Interactions with Chiral Plasmonic Nanostructures
摘要： Protein?protein interactions (PPIs) play a pivotal role in many biological processes. Discriminating functionally important well-defined protein?protein complexes formed by specific interactions from random aggregates produced by nonspecific interactions is therefore a critical capability. While there are many techniques which enable rapid screening of binding affinities in PPIs, there is no generic spectroscopic phenomenon which provides rapid characterization of the structure of protein?protein complexes. In this study we show that chiral plasmonic fields probe the structural order and hence the level of PPI specificity in a model antibody?antigen system. Using surface-immobilized Fab′ fragments of polyclonal rabbit IgG antibodies with high specificity for bovine serum albumin (BSA), we show that chiral plasmonic fields can discriminate between a structurally anisotropic ensemble of BSA-Fab′ complexes and random ovalbumin (OVA)-Fab′ aggregates, demonstrating their potential as the basis of a useful proteomic technology for the initial rapid high-throughput screening of PPIs.
关键词： specificity,Protein?protein interactions,structural order,chiral plasmonic nanostructures,high-throughput screening
更新于2025-09-16 10:30:52