Publications
2024
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(2024) Nature Communications. 15, 1, 6671. Abstract
Silk fibers unique mechanical properties have made them desirable materials, yet their formation mechanism remains poorly understood. While ions are known to support silk fiber production, their exact role has thus far eluded discovery. Here, we use cryo-electron microscopy coupled with elemental analysis to elucidate the changes in the composition and spatial localization of metal ions during silk evolution inside the silk gland. During the initial protein secretion and storage stages, ions are homogeneously dispersed in the silk gland. Once the fibers are spun, the ions delocalize from the fibroin core to the sericin-coating layer, a process accompanied by protein chain alignment and increased feedstock viscosity. This change makes the protein more shear-sensitive and initiates the liquid-to-solid transition. Selective metal ion doping modifies silk fibers mechanical performance. These findings enhance our understanding of the silk fiber formation mechanism, laying the foundations for developing new concepts in biomaterial design.
(2024) AIP Advances. 14, 11, 115301. Abstract[All authors]Minority carrier diffusion length in undoped p-type gallium oxide was measured at various temperatures as a function of electron beam charge injection by electron beam-induced current technique in situ using a scanning electron microscope. The results demonstrate that charge injection into p-type β-gallium oxide leads to a significant linear increase in minority carrier diffusion length followed by its saturation. The effect was ascribed to trapping of non-equilibrium electrons (generated by a primary electron beam) on metastable native defect levels in the material, which in turn blocks recombination through these levels. While previous studies of the same material were focused on probing a non-equilibrium carrier recombination by purely optical means (cathodoluminescence), in this work, the impact of charge injection on minority carrier diffusion was investigated. The activation energy of ∼0.072 eV, obtained for the phenomenon of interest, is consistent with the involvement of Ga vacancy-related defects.
(2024) Proceedings of the National Academy of Sciences - PNAS. 121, 34, e231551012. Abstract[All authors]Mechanical energy, specifically in the form of ultrasound, can induce pressure variations and temperature fluctuations when applied to an aqueous media. These conditions can both positively and negatively affect protein complexes, consequently altering their stability, folding patterns, and self-assembling behavior. Despite much scientific progress, our current understanding of the effects of ultrasound on the self-assembly of amyloidogenic proteins remains limited. In the present study, we demonstrate that when the amplitude of the delivered ultrasonic energy is sufficiently low, it can induce refolding of specific motifs in protein monomers, which is sufficient for primary nucleation; this has been revealed by MD. These ultrasound-induced structural changes are initiated by pressure perturbations and are accelerated by a temperature factor. Furthermore, the prolonged action of low-amplitude ultrasound enables the elongation of amyloid protein nanofibrils directly from natively folded monomeric lysozyme protein, in a controlled manner, until it reaches a critical length. Using solution X-ray scattering, we determined that nanofibrillar assemblies, formed either under the action of sound or from natively fibrillated lysozyme, share identical structural characteristics. Thus, these results provide insights into the effects of ultrasound on fibrillar protein self-assembly and lay the foundation for the potential use of sound energy in protein chemistry.
(2024) Angewandte Chemie - International Edition. 63, 14, e202318365. AbstractProtein self-assembly is a fundamental biological process where proteins spontaneously organize into complex and functional structures without external direction. This process is crucial for the formation of various biological functionalities. However, when protein self-assembly fails, it can trigger the development of multiple disorders, thus making understanding this phenomenon extremely important. Up until recently, protein self-assembly has been solely linked either to biological function or malfunction; however, in the past decade or two it has also been found to hold promising potential as an alternative route for fabricating materials for biomedical applications. It is therefore necessary and timely to summarize the key aspects of protein self-assembly: how the protein structure and self-assembly conditions (chemical environments, kinetics, and the physicochemical characteristics of protein complexes) can be utilized to design biomaterials. This minireview focuses on the basic concepts of forming supramolecular structures, and the existing routes for modifications. We then compare the applicability of different approaches, including compartmentalization and self-assembly monitoring. Finally, based on the cutting-edge progress made during the last years, we summarize the current knowledge about tailoring a final function by introducing changes in self-assembly and link it to biomaterials performance.
(2024) ACS Applied Materials and Interfaces. 16, 7, p. 9210-9223 Abstract[All authors]Biology resolves design requirements toward functional materials by creating nanostructured composites, where individual components are combined to maximize the macroscale material performance. A major challenge in utilizing such design principles is the trade-off between the preservation of individual component properties and emerging composite functionalities. Here, polysaccharide pectin and silk fibroin were investigated in their composite form with pectin as a thermal-responsive ion conductor and fibroin with exceptional mechanical strength. We show that segregative phase separation occurs upon mixing, and within a limited compositional range, domains ∼50 nm in size are formed and distributed homogeneously so that decent matrix collective properties are established. The composite is characterized by slight conformational changes in the silk domains, sequestering the hydrogen-bonded β-sheets as well as the emergence of randomized pectin orientations. However, most dominant in the composites properties is the introduction of dense domain interfaces, leading to increased hydration, surface hydrophilicity, and increased strain of the composite material. Using controlled surface charging in X-ray photoelectron spectroscopy, we further demonstrate Ca ions (Ca2+) diffusion in the pectin domains, with which the fingerprints of interactions at domain interfaces are revealed. Both the thermal response and the electrical conductance were found to be strongly dependent on the degree of composite hydration. Our results provide a fundamental understanding of the role of interfacial interactions and their potential applications in the design of material properties, polysaccharide-protein composites in particular.