Synthetic viral nanostructures are useful as materials for analyzing the biological behavior of natural viruses and as vaccine materials. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped virus embedding a spike (S) protein involved in host cell infection. Although nanomaterials modified with an S protein without an envelope membrane have been developed, they are considered unsuitable for stability and functionality. We previously constructed an enveloped viral replica complexed with a cationic lipid bilayer and an anionic artificial viral capsid self-assembled from β-annulus peptides. In this study, we report the first example of an enveloped viral replica equipped with an S protein derived from SARS-CoV-2. Interestingly, even the S protein equipped on the enveloped viral replica bound strongly to the free angiotensin-converting enzyme 2 (ACE2) receptor as well as ACE2 localized on the cell membrane.

As a natural low-calorie sweetener, Mogroside V (Mog-V) has gradually become one of the alternatives to sucrose with superior health attributes. However, Mog-V will bring unpleasant aftertastes when exceeding a threshold concentration. To investigate the possibility of soy protein isolates (SPIs), namely β-conglycinin (7S), and glycinin (11S) as flavor-improving agents of Mog-V, the binding mechanism between Mog-V and SPIs was explored through multi-spectroscopy, particle size, zeta potential, and computational simulation. The results of the multi-spectroscopic experiments indicated that Mog-V enhanced the fluorescence of 7S/11S protein in a static mode. The binding affinity of 7S-Mog-V was greater compared with 11S-Mog-V. Particle size and zeta potential analysis revealed that the interaction could promote aggregation of 7S/11S protein with different stability. Furthermore, computational simulations further confirmed that Mog-V could interact with the 7S/11S protein in different ways. This research provides a theoretical foundation for the development and application of SPI to improve the flavor of Mog-V, opening a new avenue for further expanding the market demand for Mog-V.

The enzymatic efficiency of β-glucosidases is influenced by their binding behavior onto insoluble substrates (cellulose and lignin) during bioconversion of lignocellulose. This study suggested that the Bgl3 protein (Aspergillus fumigatus) showed strong adsorption affinity to lignin and the Bgl1 protein (Penicillium oxalicum) tended to adsorb to cellulose. It indicated that the various surface properties of the fibronectin type Ш-like domain (FnIII) led to different binding properties of β-glucosidases by investigating their binding mechanism. By engineering β-glucosidases\' FnIII domain, Bgl3-1 and Bgl1-3 were constructed, which both showed lower binding capacities to insoluble substrates. As well as for Bgl1-3, its sensitivity to the phenolic component was also eased. Based on that, the reconstructed protein showed high catalytic efficiency during the enzymatic hydrolysis of corn stover by effectively transforming cellobiose to glucose. Thus, this study provided a new strategy to engineer β-glucosidases to enhance their performance in the cellulase system.

Paeonol, as one effective tyrosinase inhibitor, had been used as food preservative and clinical medication for skin disorders. In this study, the inhibition mechanism and binding behavior of paeonol to tyrosinase and its anti-browning property were investigated using multi-spectroscopic and molecular docking methods. Activity assay and kinetic results confirmed paeonol as a reversible mixed-type tyrosinase inhibitor. Results of the mechanistic studies were clarified using fluorescence quenching, synchronous fluorescence, CD spectra and 3D fluorescence, and showed that the binding of paeonol to tyrosinase might change the chromophore microenvironment and conformation of tyrosinase to inhibit enzyme catalytic activity. Molecular docking results revealed the detailed binding between paeonol and tyrosinase. Moreover, paeonol could prevent the browning of fresh-cut apples, as well as inhibiting PPO and POD activities and increasing APX activity. All above findings established a reliable basis for the inhibitory mechanism of paeonol against tyrosinase and therefore contributed to its application in anti-browning.

Cyanidin, peonidin and cyanidin-3-galactoside are the common anthocyanins with a variety of biological activities. Tyrosinase is a speed-limiting enzyme associated with melanin production. The inhibition of tyrosinase activity can prevent melanin disease while contributing to whitening. The interaction behaviors of the three anthocyanins against tyrosinase have been discussed in this paper. Cyanidin has strongest inhibitory effect on tyrosinase, and then peonidin, cyanidin-3-galactoside. Furthermore, the inhibition of tyrosinase by the three anthocyanins is mixed modes. The three anthocyanins can induce the static fluorescence quenching of tyrosinase. Cyanidin exhibits strongest binding affinity on tyrosinase, and then peonidin, cyanidin-3-galactoside based on Ka values obtain by fluorescence analysis. The binding of all anthocyanin to tyrosinase induce its conformation changes. According to molecular docking and fluorescence studies, they bind to tyrosinase by hydrogen bond and van der Waals force. In addition, the optimal modes of the three anthocyanins with tyrosinase are predicated by molecular docking. This work emphasizes that cyanidin, peonidin and cyanidin-3-galactoside may be potential drugs for the treatment of diseases caused by melanin.

Lipid binding has been proposed to represent a functional property of many allergenic proteins. This study investigated the formation, characterization, and antigenicity of lecithin-β-conglycinin complexes. The results indicate that lecithin was combined with β-conglycinin via static quenching and primarily driven by hydrogen bonds and van der Waals forces. In addition, heat treatment reduced the antigenicity of complexes, as evidenced by changes in molecular weight and secondary and tertiary structures. It revealed that large aggregates developed and more hydrophobic regions were exposed for complexes after heat treatment, as well as a decrease in the β-sheet contents and an increase in the β-turn and random coil contents. Furthermore, the average particle size of the complexes increased with increased temperature treatment, and the morphology of the complexes exhibited an amorphous polymer. These findings shedlight on the interaction between lecithin and β-conglycinin and help us understand the role of lecithin in allergic reactions.

In this study, high pressure processing (HPP) and thermal treatment were comparatively evaluated by examining their impacts on the binding behavior and interaction between α-lactalbumin (α-La) and pelargonium-3-glucoside (P3G) under pH values of 6.0, 7.4, and 8.0. The methods of circular dichroism spectroscopy, fluorescence quenching, dynamic light scattering, and molecular simulation were used to characterize the effects of processing-induced changes in protein structure, size distribution, binding site conformation, and residue charges on their binding characteristics between them. The results indicated that the thermal treatments significantly increased the quenching constants of the complex at pH 7.4/8.0 and 60/80 °C, as well as the accessible fraction of protein at pH 8.0/80 °C. Both HPP and thermal treatments increased the random coil content and showed limited effects on the α-helix and β-sheet contents of α-La and caused the aggregation of the complex to varying degrees. Molecular dynamic simulation and docking analyses revealed that the binding site of the complex did not change under different processing conditions, but the solvent-accessible surface area varied under different conditions.

The hydrolysate species of metal-based coagulants and the binding sites of humic acid (HA) are highly dependent on the pH conditions. Exploring the binding sites and modes between coagulant hydrolysates and HA molecules is critical to understanding the coagulation mechanism. In this paper, the binding behavior between HA molecules and the hydrolysates of a polyaluminum-titanium chloride composite coagulant (PATC) was investigated under different pH conditions by semi-quantitative FTIR and XPS. It was found that oligomeric and mesopolymeric hydrolysates were the dominant species under acid conditions, which could complex with the hydroxyl and carboxyl groups of HA by forming COAl/Ti coordinate bonds. However, large amounts of H+ could compete with Al3+ and weaken the removal efficiency of HA. With the increase of pH, the hydrolysis process of the PATC and the deprotonation of HA were simultaneously underway. Under weakly acid conditions, the complexation of the aluminum hydrolysates with carboxyl groups was improved due to the gradually diminishing competition of H+ and the enhanced charge neutralization of the further polymerized hydrolysates. Consequently, the maximum UV254 removal by adding PATC was observed at pH 6. Under alkaline conditions, the sweeping effect of amorphous hydroxide dominated the HA removals, which was accompanied by the surface complexation of Al/Ti nuclear with carboxyl groups as well as the hydrogen bonds between hydroxyl and hydroxide. This study provides a new clue for the interaction mechanisms between the hydrolysates of composite coagulants and the dominant functional groups of HA at various pH conditions.

Hyperoside (HYP) is an important natural product that is widely distributed in fruits and whole grasses of various plants. It is also used by consumers as a healthy ingredient. This work explored the interaction mechanisms between HYP and two main soy proteins, namely, β-conglycinin (7S) and glycinin (11S), using computational simulation and multi-spectroscopic technology. In this study, the docking and dynamic simulation showed that HYP was stable in the hydrophobic pockets of the proteins. The conformation and microenvironment of 7S/11S also changed after binding to HYP. The binding of HYP to 7S/11S was a state quenching with a good affinity at 4 °C. This result was determined from the binding constant values of (1.995 ± 0.170) × 107 M-1 and (2.951 ± 0.109) × 107 M-1, respectively. The 7S/11S-HYP complex delineated here will provide a novel idea to construct an embedding and delivery system in improving the benefits of HYP for the development of high value-added food products.

Ceritinib is a second-generation anaplastic lymphoma kinase (ALK) inhibitor for mainly treating non-small cell lung cancer (NSCLC). This investigation focused on to clarify in detail the binding behavior between human α-1 acid glycoprotein (HAG) and ceritinib by means of multi-spectroscopic and molecular modeling approaches. Fluorescence data obtained at four different temperatures indicated ceritinib quenched the endogenous fluorescence of HAG by a static quenching mechanism. Based on the Kb value at 105 M-1 level, it can be inferred that the binding affinity between both is strong. From findings of thermodynamic parameter analysis, the competitive experiments with ANS and sucrose as well as molecular dynamic (MD) simulation, it can be inferred that hydrophobicity, hydrogen bonding, van der Waals forces as well as electrostatic interactions exist in the binding interaction between ceritinib and HAG. The findings from UV absorption, circular dichroism, and synchronous fluorescence spectroscopy indicated that the change in the microenvironment around the protein structure, secondary structure and tryptophan residues occurred after interaction with ceritinib. The data from FRET analysis confirmed that the non-radiative energy transfer between the two existed and the binding distance between the acceptor (ceritinib) and donor (HAG) was 2.11 nm. Meantime, the influence of Ca2+, Cu2+, Ni2+, Co2+, and Zn2+ ions on the binding interaction of ceritinib with HAG were obvious, especially Zn2+ ion.