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69 result(s) for "Cho, Seunghee"
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Synergistic SERS Enhancement in GaN‐Ag Hybrid System toward Label‐Free and Multiplexed Detection of Antibiotics in Aqueous Solutions
Noble metal‐based surface‐enhanced Raman spectroscopy (SERS) has enabled the simple and efficient detection of trace‐amount molecules via significant electromagnetic enhancements at hot spots. However, the small Raman cross‐section of various analytes forces the use of a Raman reporter for specific surface functionalization, which is time‐consuming and limited to low‐molecular‐weight analytes. To tackle these issues, a hybrid SERS substrate utilizing Ag as plasmonic structures and GaN as charge transfer enhancement centers is presented. By the conformal printing of Ag nanowires onto GaN nanopillars, a highly sensitive SERS substrate with excellent uniformity can be fabricated. As a result, remarkable SERS performance with a substrate enhancement factor of 1.4 × 1011 at 10 fM for rhodamine 6G molecules with minimal spot variations can be realized. Furthermore, quantification and multiplexing capabilities without surface treatments are demonstrated by detecting harmful antibiotics in aqueous solutions. This work paves the way for the development of a highly sensitive SERS substrate by constructing complex metal‐semiconductor architectures. The synergistic interplay of the electromagnetic and chemical enhancement of Raman signals is achieved in an Ag nanowire/GaN nanopillar‐based hybrid SERS structure to maximize signal intensities. Using the solvent‐assisted nanotransfer printing technique, highly ordered metal nanostructures are fabricated conformally on a nanopatterned semiconductor substrate. Therefore, several antibiotics dissolved in aqueous solutions are detected without any Raman reporters.
Novel method for modified interlaminar approach using contralateral oblique view: A technical suggestion
A modified interlaminar (MIL) approach has been proposed for improved accessibility to the target epidural space. However, even with fluoroscopic guidance, uncertainty about the distance between the needle tip and the epidural space can remain. Using the contralateral oblique (CLO) view, determination of the epidural space can be easier with clearer identification of the interlaminar opening. We inserted the needle at the midpoint of the interlaminar opening on the fluoroscopic anteroposterior (AP) view and made the needle oriented toward the pedicle of the target side. Then, CLO view was created by rotating the intensifier approximately 45 degrees to the contralateral side of the target. Through the CLO view, the ventral interlaminar line (VILL) was confirmed and the needle was able to enter the epidural space more easily. The medical records of 29 patients who were conducted MIL approach using CLO view were retrospectively analyzed to evaluate the effectiveness and safety of this procedure. The accessibility to the ventral epidural space was 93.1%. There was no procedure-related complication. Using CLO view, uncertainty can be reduced during the MIL approach, which in turn shortens procedure time and improves safety.
Minimizing quantification uncertainty in nanoplasmonic platforms: Multifunctional MoS2‐integration for precise biomarker determination
Despite growing interest in nanoplasmonic biosensors—particularly surface‐enhanced Raman spectroscopy (SERS) platforms—their potential has been limited by high quantification variability rooted in poor uniformity. Previous approaches to address this, such as incorporating internal standards (ISs), often sacrificed sensitivity for uniformity or lacked a clear analytical basis for accurate quantification. Here, a novel approach of integrating MoS2 into a SERS platform is introduced, with a focus on mitigating spot‐to‐spot relative standard deviation (RSD) and improving quantification accuracy. While maintaining the well‐known enhanced sensitivity of MoS2, the Raman signal from a uniform monolayer is utilized to calibrate signal variations. As a result, the platform achieves the lowest RSD (5.29%) among MoS2‐based systems, while offering the highest level of sensitivity in rhodamine 6G (R6G) measurements. For albumin, the target proteinuria biomarker, MoS2‐based normalization outperforms conventional wafer‐based methods and achieves a 42% RSD reduction over non‐normalization because the atomic thickness MoS2 enables precise plasmonic calibration. Furthermore, a consistent, exponential relationship between MoS2 signal intensity and albumin concentration is discovered. Quantification trends are consequently highly predictable, resulting in a 4.8‐fold increase in data separability. This quantification approach is shown to be effective for albumin mixed in artificial urine under various laser conditions, highlighting the practical potential of our platform for early‐stage monitoring of biomarkers. The multifunctional integration of MoS2 into the SERS platform addresses key limitations in accurate quantification. Atomically thin MoS2 reduces spot‐to‐spot variations via plasmonic calibration and improves quantification reliability by ensuring consistent signal changes with analyte concentration. These advances enable precise detection of low‐concentration albumin for early‐stage monitoring of proteinuria.
Highly Tunable, Nanomaterial‐Functionalized Structural Templating of Intracellular Protein Structures Within Biological Species
Inside living organisms, proteins are self‐assembled into diverse 3D structures optimized for specific functions. This structure‐function relationship can be exploited to synthesize functional materials through biotemplating and depositing functional materials onto protein structures. However, conventional biotemplating faces limitations due to the predominantly intracellular existence of proteins and associated challenges in achieving tunability while preserving functionality. In this study, Conversion to Advanced Materials via labeled Biostructures (CamBio), an integrated biotemplating platform that involves labeling target protein structures with antibodies followed by the growth of functional materials, ensuring outstanding nanostructure tunability is proposed. Protein‐derived plasmonic nanostructures created by CamBio can serve as precise quantitative tools for assessing target species is demonstrated. The assessment is achieved through highly tunable and efficient surface‐enhanced Raman spectroscopy (SERS). CamBio enables the formation of dense nanogap hot spots among metal nanoparticles, templated by diverse fibrous proteins comprising densely repeated monomers. Furthermore, iterative antibody labeling strategies to adjust the antibody density surrounding targets, amplifying the number of nanogaps and consequently improving SERS performance are employed. Finally, cell‐patterned substrates and whole meat sections as SERS substrates, confirming their easily accessible, cost‐effective, scalable preparation capabilities and dimensional tunability are incorporated. This work demonstrates an integrated biotemplating that utilizes intracellular proteins to fabricate highly functional nanomaterials, called Conversion to advanced materials via labeled Biostructures (CamBio). This work exploits the structural characteristics of cells and tissues, employing them as Surface‐Enhanced Raman Spectroscopy (SERS) substrates by combining conventional fabrication and bio‐related techniques. This work offers the capability to transform advanced materials by adding biostructural benefits for a myriad of applications.
Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis
An ancient enzyme family responsible for the catabolism of the prebiotic chemical cyanuric acid (1,3,5-triazine-2,4,6-triol) was recently discovered and is undergoing proliferation in the modern world due to industrial synthesis and dissemination of 1,3,5-triazine compounds. Cyanuric acid has a highly stabilized ring system such that bacteria require a unique enzyme with a novel fold and subtle active site construction to open the ring. Each cyanuric acid hydrolase monomer consists of three isostructural domains that coordinate and activate the three-fold symmetric substrate cyanuric acid for ring opening. We have now solved a series of X-ray structures of an engineered, thermostable cyanuric acid ring-opening enzyme at 1.51 ~ 2.25 Å resolution, including various complexes with the substrate, a tight-binding inhibitor, or an analog of the reaction intermediate. These structures reveal asymmetric interactions between the enzyme and bound ligands, a metal ion binding coupled to conformational changes and substrate binding important for enzyme stability, and distinct roles of the isostructural domains of the enzyme. The multiple conformations of the enzyme observed across a series of structures and corroborating biochemical data suggest importance of the structural dynamics in facilitating the substrate entry and the ring-opening reaction, catalyzed by a conserved Ser-Lys dyad.
3′-Sialyllactose alleviates bone loss by regulating bone homeostasis
Osteoporosis is a common skeletal disease that results in an increased risk of fractures. However, there is no definitive cure, warranting the development of potential therapeutic agents. 3′-Sialyllactose (3′-SL) in human milk regulates many biological functions. However, its effect on bone metabolism remains unknown. This study aimed to investigate the molecular mechanisms underlying the effect of 3′-SL on bone homeostasis. Treatment of human bone marrow stromal cells (hBMSCs) with 3′-SL enhanced osteogenic differentiation and inhibited adipogenic differentiation of hBMSCs. RNA sequencing showed that 3′-SL enhanced laminin subunit gamma-2 expression and promoted osteogenic differentiation via the phosphatidylinositol 3‑kinase/protein kinase B signaling pathway. Furthermore, 3′-SL inhibited the receptor activator of nuclear factor κB ligand-induced osteoclast differentiation of bone marrow-derived macrophages through the nuclear factor κB and mitogen‑activated protein kinase signaling pathway, ameliorated osteoporosis in ovariectomized mice, and positively regulated bone remodeling. Our findings suggest 3′-SL as a potential drug for osteoporosis. 3′-Sialyllactose alleviates the progression of osteoporosis by regulating bone homeostasis and may have a therapeutic effect as an anti-osteoporosis agent.
Effective Chemical Lift-Off for Air-Tunnel GaN on a Trapezoid-Patterned Sapphire Substrate
We fabricated an air-tunnel structure between a gallium nitride (GaN) layer and trapezoid-patterned sapphire substrate (TPSS) through the in situ carbonization of a photoresist layer to enable rapid chemical lift-off (CLO). A trapezoid-shaped PSS was used, which is advantageous for epitaxial growth on the upper c-plane when forming an air tunnel between the substrate and GaN layer. The upper c-plane of the TPSS was exposed during carbonization. This was followed by selective GaN epitaxial lateral overgrowth using a homemade metal organic chemical vapor deposition system. The air tunnel maintained its structure under the GaN layer, whereas the photoresist layer between the GaN layer and TPSS disappeared. The crystalline structures of GaN (0002) and (0004) were investigated using X-ray diffraction. The photoluminescence spectra of the GaN templates with and without the air tunnel showed an intense peak at 364 nm. The Raman spectroscopy results for the GaN templates with and without the air tunnel were redshifted relative to the results for free-standing GaN. The CLO process using potassium hydroxide solution neatly separated the GaN template with the air tunnel from the TPSS.
Cyanuric Acid Hydrolase from Azorhizobium caulinodans ORS 571: Crystal Structure and Insights into a New Class of Ser-Lys Dyad Proteins
Cyanuric acid hydrolase (CAH) catalyzes the hydrolytic ring-opening of cyanuric acid (2,4,6-trihydroxy-1,3,5-triazine), an intermediate in s-triazine bacterial degradation and a by-product from disinfection with trichloroisocyanuric acid. In the present study, an X-ray crystal structure of the CAH-barbituric acid inhibitor complex from Azorhizobium caulinodans ORS 571 has been determined at 2.7 Å resolution. The CAH protein fold consists of three structurally homologous domains forming a β-barrel-like structure with external α-helices that result in a three-fold symmetry, a dominant feature of the structure and active site that mirrors the three-fold symmetrical shape of the substrate cyanuric acid. The active site structure of CAH is similar to that of the recently determined AtzD with three pairs of active site Ser-Lys dyads. In order to determine the role of each Ser-Lys dyad in catalysis, a mutational study using a highly sensitive, enzyme-coupled assay was conducted. The 10⁹-fold loss of activity by the S226A mutant was at least ten times lower than that of the S79A and S333A mutants. In addition, bioinformatics analysis revealed the Ser226/Lys156 dyad as the only absolutely conserved dyad in the CAH/barbiturase family. These data suggest that Lys156 activates the Ser226 nucleophile which can then attack the substrate carbonyl. Our combination of structural, mutational, and bioinformatics analyses differentiates this study and provides experimental data for mechanistic insights into this unique protein family.
The effects of social concern goals on the value of learning and on the intentions of medical students to change their majors
Background: In the process of developing a professional medical expertise, goals can become a psychological impetus and act as a source of retaining an individual's persistency. Therefore, the goals of medical students should be considered when designing a curriculum for health professions. Purpose: The purpose of this study was to examine relative effects of goal categories on the value of learning and intention to change one's major. Method: Data were obtained from the Korea Education Longitudinal Study, which included 1938 representative Korean college freshmen majoring in medicine, engineering, natural science and humanities. They answered a survey questionnaire about goal categories (i.e., social concern, affiliation, self-growth, leisure, wealth, and fame), the value of learning, and intention to change one's major. Results: For medical students, social concern goals were positively related to the value of learning and negatively related to the intention to change one's major. Social concern goals decreased the intention to change one's major directly, and also indirectly through increased value of learning. Conclusion: Providing context for enhancing medical students' social concern goals is necessary in a medical training curriculum, not only for the students' professional development but also for improving society. Abbreviations: GCT: Goal contents theory GPA: Grade point average KELS: Korea education longitudinal study SDLA: Self-directed learning abilities SDT: Self-determination theory
Highly Transparent Spectral Tunable Electrochromic Window Based on Solid-State WO3 Thin Films
Energy conservation is crucial for sustainable growth. Electrochromic window devices, which regulate optical transmittance using light-tunable materials like WO3, can significantly reduce both thermal and visual energy consumption in buildings. In this study, we developed solid-state WO3 thin film-based electrochromic window using room-temperature sputtering. The WO3 film was grown through reactive sputtering of a tungsten target, resulting in highly transparent films with structural and optical properties well-suitable for electrochromic devices. These films exhibit efficient coloration and fast response times. WO3-based electrochromic devices offer superior modulation across ultraviolet, visible, and infrared (IR) wavelengths, blocking over 95% of IR wavelengths. Key performance metrics include a coloration efficiency of 96.96 cm2 C−1, optical modulation of 68.5% in the visible region, reversibility of 88.1%, and response time of 10 s (coloration time) and 24 s (bleaching time). These results highlight the potential of WO3-based electrochromic windows for energy conservation, making them ideal for integration into building structures as energy-sustainable entities.