Multiphoton emission of single CdZnSe/ZnS quantum dots coupled with plasmonic Au nanoparticles.

The fluorescence blinking and low multiphoton emission of quantum dots (QDs) have limited their application in lasing, light-emitting diodes, and so on. Coupling of single QDs to plasmonic nanostructures is an effective approach to control the photon properties. Here plasmon-exciton systems including Au nanoparticles and CdZnSe/ZnS QDs were investigated at the single particle level. With the modulation of the local electromagnetic field, the fluorescence intensity of single QDs is increased, accompanied by a significant suppression in blinking behavior, and the lifetime is shortened from 15 ns to 2 ns. Moreover, the second-order photon intensity correlation at zero lag time g2(0) of coupled single QDs is larger than 0.5, indicating an increased probability of multiphoton emission. The enhancement factors of radiative and nonradiative decay rates of QDs coupled with Au nanoparticles are calculated. The sharply increased radiative decay rate can be comparable to the nonradiative Auger rate, leading to dominated multiple exciton radiative recombination with PL intensity enhancement, suppressed blinking, lifetime shortening, and multiphoton emission. The results of the exciton decay dynamics and emission properties of single QDs in this work are helpful in exploring the mechanism of plasmon-exciton interaction and optoelectronic application of single QDs.

Mechanistic insight into E22Q-mutation-induced antiparallel-to-parallel ß-sheet transition of Aß16-22 fibrils: an all-atom simulation study.

Alzheimer's disease is associated with the abnormal self-assembly of amyloid-ß (Aß) peptide into toxic oligomers and fibrils. Recent experiments reported that Aß16-22, containing the central hydrophobic core (CHC) of Aß, formed antiparallel ß-sheet fibrils, while its E22Q mutant self-assembled into parallel ß-sheet fibrils. However, the molecular mechanisms underlying E22Q-mutation-induced parallel ß-sheet fibril formation are not well understood. Herein, we performed molecular dynamics (MD) simulations to study the dimerization processes of Aß16-22 and Aß16-22E22Q peptides. ß-Sheet dimers with diverse hydrogen bond arrangements were observed and they exhibited highly dynamic and interconverting properties. An antiparallel-to-parallel ß-sheet transition occurred in the assembly process of the E22Q mutant, but not in that of Aß16-22. During this conformational transformation process, the inter-molecular Q22-Q22 hydrogen bonds were first formed and acted as a binder to facilitate the two chains forming a parallel orientation, then the hydrophobic interactions between residues in the CHC region consolidated this arrangement and drove the main-chain H-bond formation, hence resulting in parallel ß-sheet formation. However, parallel ß-sheets were less populated than antiparallel ß-sheets of Aß16-22E22Q dimers. In order to explore whether parallel ß-sheets became dominant in larger size oligomers, we investigated the conformational ensembles of Aß16-22 and Aß16-22E22Q octamers by conducting replica exchange molecular dynamics (REMD) simulations. The REMD simulations revealed that the population of parallel ß-strand alignment increased with an increase of the size of ordered Aß16-22E22Q ß-sheet oligomers, implying that the formation of full parallel ß-sheets requires larger sized oligomers. Our findings provide a mechanistic explanation for the E22Q-mutation-induced formation of parallel ß-sheet fibrils observed experimentally.

Influence of fullerenol on hIAPP aggregation: amyloid inhibition and mechanistic aspects.

Fullerenols have garnered significant scientific interest in nano-technology and biomedicine. A detailed understanding of their interactions with proteins is fundamentally important for their biomedical applications. Human islet amyloid polypeptide (hIAPP) is an intrinsically disordered protein and its aggregation is associated with type 2 diabetes. Here, we investigated the nano-bio-interactions of fullerenol with hIAPP and focused on the effect of C60(OH)24 on hIAPP aggregation by replica-exchange molecular dynamic simulations. Our simulations show that isolated hIAPP dimers transiently populated amyloid-precursor (ß-hairpin) containing ß-sheet structure, whereas C60(OH)24 completely suppressed this fibril-prone structure, thus inhibiting hIAPP aggregation. The simulation-predicted inhibitory effect of fullerenols was validated by atom force microscopy and thioflavin T fluorescence experiments. We find C60(OH)24 binds to hIAPP via hydrogen bonding interactions with polar residues T9, Q10, N14, N21, N22, N31, N35 and T36 as well as the collective van der Waals and hydrogen-bonding interaction with Y37. Molecular dynamic simulations show that C60(OH)24 destabilized the hIAPP protofibril by mostly binding to the 20SNNFGAILSS29 amyloid core region. This study not only helps to understand the mechanisms involved in hIAPP aggregation and amyloid inhibition, but also provides new clues for the development of therapeutic candidates against type 2 diabetes.

Effects of hydroxylated carbon nanotubes on the aggregation of Aß16-22 peptides: a combined simulation and experimental study.

The pathogenesis of Alzheimer's disease (AD) is associated with the aggregation of amyloid-ß (Aß) peptides into toxic aggregates with ?-sheet character. In a previous computational study, we showed that pristine single-walled carbon nanotubes (SWCNTs) can inhibit the formation of ß-sheet-rich oligomers in the central hydrophobic core fragment of Aß (Aß16-22). However, the poor solubility of SWCNTs in water hinders their use in biomedical applications and nanomedicine. Here, we investigate the influence of hydroxylated SWCNT, a water-soluble SWCNT derivative, on the aggregation of Aß16-22 peptides using all-atom explicit-water replica exchange molecular dynamics simulations. Our results show that hydroxylated SWCNTs can significantly inhibit ß-sheet formation and shift the conformations of Aß16-22 oligomers from ordered ß-sheet-rich structures toward disordered coil aggregates. Detailed analyses of the SWCNT-Aß interaction reveal that the inhibition of ß-sheet formation by hydroxylated SWCNTs mainly results from strong electrostatic interactions between the hydroxyl groups of SWCNTs and the positively charged residue K16 of Aß16-22 and hydrophobic and aromatic stacking interactions between SWCNTs and F19 and F20. In addition, our atomic force microscopy and thioflavin T fluorescence experiments confirm the inhibitory effect of both pristine and hydroxylated SWCNTs on Aß16-22 fibrillization, in support of our previous and present replica exchange molecular dynamics simulation results. These results demonstrate that hydroxylated SWCNTs efficiently inhibit the aggregation of Aß16-22; in addition, they offer molecular insight into the inhibition mechanism, thus providing new clues for the design of therapeutic drugs against amyloidosis.

One-Step Hydrothermal Synthesis of Highly Fluorescent MoS2 Quantum Dots for Lead Ion Detection in Aqueous Solutions.

Lead ions in water are harmful to human health and ecosystems because of their high toxicity and nondegradability. It is important to explore effective fluorescence probes for Pb2+ detection. In this work, surface-functionalized molybdenum disulfide quantum dots (MoS2 QDs) were prepared using a hydrothermal method, and ammonium tetrathiomolybdate and glutathione were used as precursors. The photoluminescence quantum yield of MoS2 QDs can be improved to 20.4%, which is higher than that for MoS2 QDs reported in current research. The as-prepared MoS2 QDs demonstrate high selectivity and sensitivity for Pb2+ ions, and the limit of detection is 0.056 µM. The photoluminescence decay dynamics for MoS2 QDs in the presence of Pb2+ ions in different concentrations indicate that the fluorescence quenching originated from nonradiative electron transfer from excited MoS2 QDs to the Pb2+ ion. The prepared MoS2 QDs have great prospect and are expected to become a good method for lead ion detection.

The Lattice Distortion, Defect Evolution and Electrochemical Performance Improvement in Zn-VO2(B) Nanorods.

Cathode materials of energy storage batteries have attracted extensive attention because of the importance in deciding the rate performance and long cycle property of batteries. Herein, we report a simple and environmentally friendly solvothermal method to prepare Zn-doped VO2(B) cathode materials. The introduction of zinc ions can effectively regulate the lattice structure, surface morphology and internal defect state of Zn-VO2(B) nano materials. The sample with Zn content x = 1.5% has smaller cell volume and grain size, and higher concentration of vacancy defects. These microstructures ensure the structural stability during ion embedding process and, thus, this sample shows excellent electrochemical performances. The capacitance retention rate still maintains 88% after 1000 cycles at the current density of 0.1 A·g-1. The enhanced performances of Zn-doped VO2(B) samples may lay a foundation for the improvement of electrochemical performances of VO2(B) cathode materials for energy storage batteries in the future.

The molecular mechanism of fullerene-inhibited aggregation of Alzheimer's ß-amyloid peptide fragment.

Amyloid deposits are implicated in the pathogenesis of many neurodegenerative diseases such as Alzheimer's disease (AD). The inhibition of ß-sheet formation has been considered as the primary therapeutic strategy for AD. Increasing data show that nanoparticles can retard or promote the fibrillation of amyloid-ß (Aß) peptides depending on the physicochemical properties of nanoparticles, however, the underlying molecular mechanism remains elusive. In this study, our replica exchange molecular dynamics (REMD) simulations show that fullerene nanoparticle - C60 (with a fullerene : peptide molar ratio greater than 1 : 8) can dramatically prevent ß-sheet formation of Aß(16-22) peptides. Atomic force microscopy (AFM) experiments further confirm the inhibitory effect of C60 on Aß(16-22) fibrillation, in support of our REMD simulations. An important finding from our REMD simulations is that fullerene C180, albeit with the same number of carbon atoms as three C60 molecules (3C60) and smaller surface area than 3C60, displays an unexpected stronger inhibitory effect on the ß-sheet formation of Aß(16-22) peptides. A detailed analysis of the fullerene-peptide interaction reveals that the stronger inhibition of ß-sheet formation by C180 results from the strong hydrophobic and aromatic-stacking interactions of the fullerene hexagonal rings with the Phe rings relative to the pentagonal rings. The strong interactions between the fullerene nanoparticles and Aß(16-22) peptides significantly weaken the peptide-peptide interaction that is important for ß-sheet formation, thus retarding Aß(16-22) fibrillation. Overall, our studies reveal the significant role of fullerene hexagonal rings in the inhibition of Aß(16-22) fibrillation and provide novel insight into the development of drug candidates against Alzheimer's disease.

Aß(16-22) peptides can assemble into ordered ß-barrels and bilayer ß-sheets, while substitution of phenylalanine 19 by tryptophan increases the population of disordered aggregates.

A recent experimental study reported that termini-uncapped Aß(16-22) (with sequence KLVFFAE) peptides self-assembled into nanofibrils at pH 2.0. The oligomerization of this uncapped peptide at atomic level in acidic pH condition remains to be determined, as computational studies mainly focus on the self-assembly of capped Aß(16-22) peptides at neutral pH condition. In this study, using replica exchange molecular dynamics (REMD) simulations with explicit solvent, we investigated the octameric structures of the uncapped Aß(16-22) and its F19W variant at acidic pH condition. Our simulations reveal that the Aß(16-22) octamers adopt various conformations, including closed ß-barrels, bilayer ß-sheets, and disordered aggregates. The closed ß-barrel conformation is particularly interesting, as the cylindrical ß-barrel has been reported recently as a cytotoxic species. Interpeptide contact probability analyses between all pairs of residues reveal that the hydrophobic and aromatic stacking interactions between F19 residues play an essential role in the formation of ß-barrels and bilayer ß-sheets. The importance of F19 and the steric effect on the structures of Aß(16-22) octamers are further examined by REMD simulation of F19W mutant. This REMD run shows that substitution of F19 by W with a more bulky aromatic side chain significantly reduces the ß-sheet content and in turn enhances the population of disordered aggregates, indicating that the steric effect significantly affect the self-assembly of low molecular weight Aß(16-22) oligomers.