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1.
Nano Lett ; 22(9): 3840-3847, 2022 May 11.
Artigo em Inglês | MEDLINE | ID: mdl-35500126

RESUMO

γ-indium selenide (InSe) is a van der Waals semiconductor and holds great potentials for low-energy-consumption electronic and optoelectronic devices. Herein, we investigated the hydrostatic pressure engineered near-infrared (NIR) light emission of mechanically exfoliated γ-InSe crystals using the diamond anvil cell (DAC) technique. A record-wide spectral tuning range of 185 nm and a large linear pressure coefficient of 40 nm GPa-1 were achieved for spontaneous emissions, leading to ultrabroadband microlasing spectrally ranging from 1022 to 911 nm. This high emission tunability can be attributed to the compression of the soft intralayer In-Se bonds under high pressure, which suppressed the band gap shrinkage by increasing the interlayer interaction. Furthermore, two band gap crossovers of valence (direct-to-indirect) and conduction bands were resolved at approximately 4.0 and 7.0 GPa, respectively, resulting in pressure-sensitive emission lifetime and intensity. These findings pave the pathways for pressure-sensitive InSe-based NIR light sources, sensors and so on.

2.
Food Chem ; 366: 130422, 2022 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-34392082

RESUMO

Tea cream, produced by interactions among tea ingredients, is undesirable in tea beverage industry. The interaction between bovine serum albumin (BSA) and theaflavin-3,3'-digallate (TFDG, an important component in tea cream and functional substance of black tea) was investigated by fluorescence spectroscopy, ultraviolet-visible (UV-vis) absorption spectroscopy, synchronous fluorescence spectroscopy, fourier-transform infrared (FT-IR) spectroscopy, and molecular docking technique. Multi-spectroscopic experiments demonstrated that TFDG interacted with BSA via static quenching, and the microenvironment around BSA became more hydrophobicity. FT-IR showed that the α-helix of BSA was increased when binding with TFDG. Thermodynamic parameters and molecular docking demonstrated that hydrophobic interactions and hydrogen bonds dominated the interaction between TFDG and BSA. The mechanism proposed in this research could further develop some nanoparticles to excellent biochemical properties while reducing the formation of tea cream, and explore the potential of BSA as transport carrier for TFDG.


Assuntos
Soroalbumina Bovina , Biflavonoides , Sítios de Ligação , Catequina/análogos & derivados , Dicroísmo Circular , Simulação de Acoplamento Molecular , Ligação Proteica , Soroalbumina Bovina/metabolismo , Espectrometria de Fluorescência , Espectrofotometria Ultravioleta , Espectroscopia de Infravermelho com Transformada de Fourier , Termodinâmica
3.
Food Chem ; 333: 127432, 2020 Dec 15.
Artigo em Inglês | MEDLINE | ID: mdl-32659661

RESUMO

The sensory qualities and shelf life of tea beverage strongly affected by tea cream that forms by the interaction of polyphenols and protein. The study aimed to investigate the effects of the interactions between tea polyphenols (TPs) and bovine serum albumin (BSA) on tea cream formation at different concentrations. The tea cream formation increased with TPs and BSA concentration increased. The optimal concentration (TPs: 800 mg/L, BSA: 40 mg/L), for high clarities and contents of phytochemicals, was selected by the technique for order preference by similarity to ideal solution (C = 0.7572). The interaction mechanism of TPs-BSA was investigated by fluorescence spectroscopy, UV-visible absorption spectroscopy, synchronous fluorescence spectroscopy, and molecular docking. TPs interacted with BSA via static quenching process, affecting tryptophan and tyrosine residue microenvironment of BSA. Ester catechins had more binding affinity than non-ester catechins. Hydrogen bonds were the main interaction forces of TPs-BSA.


Assuntos
Polifenóis/química , Polifenóis/metabolismo , Soroalbumina Bovina/química , Chá/química , Animais , Sítios de Ligação , Catequina/química , Catequina/metabolismo , Precipitação Química , Ligação de Hidrogênio , Simulação de Acoplamento Molecular , Tamanho da Partícula , Soroalbumina Bovina/metabolismo , Espectrometria de Fluorescência , Espectrofotometria Ultravioleta , Chá/metabolismo , Termodinâmica
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