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Over the past decade, SnO has been considered a promising p-type oxide semiconductor. However, achieving high mobility in the fabrication of p-type SnO films is still highly dependent on the post-annealing procedure, which is often used to make SnO, due to its metastable nature, readily convertible to SnO 2 and/or intermediate phases. This paper demonstrates a fully room-temperature fabrication of p-type SnO x thin films using ion-beam-assisted deposition. This technique offers independent control between ion density, via the ion-gun anode current and oxygen flow rate, and ion energy, via the ion-gun anode voltage, thus being able to optimize the optical band gap and the hole mobility of the SnO films to reach 2.70 eV and 7.89 cm 2 V -1 s -1 , respectively, without the need for annealing. Remarkably, this is the highest mobility reported for p-type SnO films whose fabrication was carried out entirely at room temperature. Using first-principles calculations, we rationalize that the high mobility is associated with the fine-tuning of the Sn-rich-related defects and lattice densification, obtained by controlling the density and energy of the oxygen ions, both of which optimize the spatial overlap of the valence bands to form a continuous conduction path for the holes. Moreover, due to the absence of the annealing process, the Raman spectra reveal no significant signatures of microcrystal formation in the films. This behavior contrasts with the case involving the air-annealing procedure, where a complex interaction occurs between the formation of SnO microcrystals and the formation of SnO x intermediate phases. This interplay results in variations in grain texture within the film, leading to a lower optimum Hall mobility of only 5.17 cm 2 V -1 s -1 . Finally, we demonstrate the rectification characteristics of all-fabricated-at-room-temperature SnO x -based p-n devices to confirm the viability of the p-type SnO x films.

Parkinson's disease (PD) is an acute and progressive neurodegenerative disorder, and diagnosis of the disease at its earliest stage is of paramount importance to improve the life expectancy of patients. α-Synuclein (α-syn) is a potential biomarker for the early diagnosis of PD, and there is a great need to develop a biosensing platform that precisely detects α-syn in human body fluids. Herein, we developed a surface plasmon resonance (SPR) biosensor based on the label-free iron oxide nanoparticles (Fe 3 O 4 NPs) and paired antibody for the highly sensitive and selective detection of α-syn in serum samples. The sensitivity of the SPR platform is enhanced significantly by directly depositing Fe 3 O 4 NPs on the Au surface at a high density to increase the decay length of the evanescent field on the Au film. Moreover, the utilization of rabbit-type monoclonal antibody (α-syn-RmAb) immobilized on Au films allows the SPR platform to have a high affinity-selectivity binding performance compared to mouse-type monoclonal antibodies as a common bioreceptor for capturing α-syn molecules. As a result, the current platform has a detection limit of 5.6 fg/mL, which is 20,000-fold lower than that of commercial ELISA. The improved sensor chip can also be easily regenerated to repeat the α-syn measurement with the same sensitivity. Furthermore, the SPR sensor was applied to the direct analysis of α-syn in serum samples. By using a format of paired α-syn-RmAb, the SPR sensor provides a recovery rate in the range from 94.5% to 104.3% to detect the α-syn in diluted serum samples precisely. This work demonstrates a highly sensitive and selective quantification approach to detect α-syn in human biofluids and paves the way for the future development in the early diagnosis of PD.

Matching the resonant wavelength of plasmonic nanoparticles (NPs) and the emission band of organic materials is critical for achieving optimal plasmon-enhanced luminescence in organic light-emitting devices (OLEDs). However, the spectral matching is often unsatisfactory because the interior architecture of OLEDs limits the dimensions of the NPs to support the desired wavelength adjustment. In this article, we proposed a design strategy via Au x Ag 1-x alloy NPs to enable resonance tuning while preserving the size of the NP to suit the OLED design requirements. The bimetallic NPs, especially for x < 0.6, not only add one more degree of freedom to vary the plasmon wavelength but also provide the benefits of higher scattering and more intense and outspread electric fields over a broader spectrum compared to Au monometallic NPs. These features allow smaller NPs, which are more compatible with OLED interiors, to scatter electric fields more efficiently and increase the density of molecules interacting with the NP plasmons. In the presence of a nearby dipole emitter, the bimetallic NPs can simultaneously increase radiative enhancement and suppress non-radiative losses, which are advantageous for increasing the quantum yield and luminescence efficiency of the emitter. These improvements are associated with lower intraband and interband activities resulting from the higher molar fraction of Ag in the alloy NPs. We provided composition mappings to achieve enhanced luminescence for specified wavelengths at fixed NP sizes. Finally, we theoretically demonstrated that the bimetallic NPs could improve the light-extraction efficiency of OLEDs better than Au monometallic NPs. This work provides essential guidance to enable versatile plasmon-enhanced applications with predefined nanostructural geometries and wavelengths to match the device requirements.

The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells. However, Flt3 is also one of the most frequently mutated receptors in hematologic malignancies and is currently a major prognostic factor and clinical target for acute myeloid leukemia. Here, we report the structural basis for the Flt3 ligand-receptor complex and unveil an unanticipated extracellular assembly unlike any other RTKIII/V complex characterized to date. FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions. Comparisons of Flt3 with homologous receptors and available mutagenesis data for FL have allowed us to rationalize the unique features of the Flt3 extracellular assembly. Furthermore, thermodynamic dissection of complex formation points to a pronounced enthalpically driven binding event coupled to an entropic penalty. Together, our data suggest that the high-affinity Flt3:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.