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  1. Abstract

    Perovskite solar cells (PSCs) have attracted great attention in both academic and industrial sectors in the past years. Studies demonstrated that processing additive engineering was a facile way to improve the crystallinity and minimize the defect of metal halide perovskites (MHPs). In this study, we report efficient and stable PSCs, where the MHPs thin film is processed with KI additives. It is found that the KI processing additives could not only enhance the crystallization and suppress the defects of MHP thin film, but also boost charge transport, suppress non-radiative recombination, and enhance the hydrophobic properties of MHP thin film. As a result, the PSCs based on the MHPs thin film processed with KI additives exhibit more than 10% enhancement in efficiency and dramatically boosted stability compared to that based on pristine MHPs thin film. Our results indicated that the MHPs processed with processing additives are a simple engineering technique to boost the device performance of PSCs.

     
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  2. Free, publicly-accessible full text available May 28, 2025
  3. Free, publicly-accessible full text available April 17, 2025
  4. Misfolding and aggregation of amyloid peptides are critical pathological events in numerous protein misfolding diseases (PMDs), such as Alzheimer's disease (AD), type II diabetes (T2D), and medullary thyroid carcinoma (MTC). While developing effective amyloid detectors and inhibitors to probe and prevent amyloid aggregation is a crucial diagnostic and therapeutic strategy for treating debilitating diseases, it is important to recognize that amyloid detection and amyloid prevention are two distinct strategies for developing pharmaceutical drugs. Here, we reported novel fluorescent BO21 as a versatile “dual-function, multi-target” amyloid probe and inhibitor for detecting and preventing amyloid aggregates of different sequences (Aβ, hIAPP, or hCT) and sizes (monomers, oligomers, or fibrils). As an amyloid probe, BO21 demonstrated a higher sensitivity and binding affinity to oligomeric and fibrillar amyloids compared to ThT, resulting in up to 18–39 fold fluorescence enhancements. As an amyloid inhibitor, BO21 also demonstrated its strong amyloid inhibition property by effectively preventing amyloid aggregation, disaggregating preformed amyloid fibrils, and reducing amyloid-induced cytotoxicity. The findings of this study offer a new perspective for the discovery of dual-functional amyloid probes and inhibitors, which have the potential to greatly expand the diagnostic and therapeutic treatments available for PMDs. 
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  5. Abstract

    The development and understanding of antifreezing hydrogels are crucial both in principle and practice for the design and delivery of new materials. The current antifreezing mechanisms in hydrogels are almost exclusively derived from their incorporation of antifreezing additives, rather than from the inherent properties of the polymers themselves. Moreover, developing a computational model for the independent yet interconnected double-network (DN) structures in hydrogels has proven to be an exceptionally difficult task. Here, we develop a multiscale simulation platform, integrating ‘random walk reactive polymerization’ (RWRP) with molecular dynamics (MD) simulations, to computationally construct a physically-chemically linked PVA/PHEAA DN hydrogels from monomers that mimic a radical polymerization and to investigate water structures, dynamics, and interactions confined in PVA/PHEAA hydrogels with various water contents and temperatures, aiming to uncover antifreezing mechanism at atomic levels. Collective simulation results indicate that the antifreezing property of PVA/PHEAA hydrogels arises from a combination of intrinsic, strong water-binding networks and crosslinkers and tightly crosslinked and interpenetrating double-network structures, both of which enhance polymer-water interactions for competitively inhibiting ice nucleation and growth. These computational findings provide atomic-level insights into the interplay between polymers and water molecules in hydrogels, which may determine their resistance to freezing.

     
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  6. Since hIAPP (human islet amyloid polypeptide) aggregation and microbial infection are recognized as significant risk factors that contribute to the pathogenesis of type II diabetes (T2D), targeting these catastrophic processes simultaneously may have a greater impact on the prevention and treatment of T2D. Different from the well-studied hIAPP inhibitors, here we propose and demonstrate a repurposing strategy for an antimicrobial peptide, aurein, which can simultaneously modulate hIAPP aggregation and inhibit microbial infection. Collective data from protein, cell, and bacteria assays revealed multiple functions of aurein including (i) promotion of hIAPP aggregation at a low molar ratio of aurein:hIAPP = 0.5 : 1–2 : 1, (ii) reduction of hIAPP-induced cytotoxicity in RIN-m5F cells, and (iii) preservation of original antimicrobial activity against E. coli., S.A., and S.E. strains in the presence of hIAPP. These functions of aurein are mainly derived from its strong binding to different hIAPP seeds through conformationally similar β-sheet association. Our study provides a promising avenue for the repurposing of antimicrobial peptides (such as aurein) as amyloid modulators for blocking at least two pathological pathways in T2D. 
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