Phosgene has attracted wide attention because of its important applications and value in modern industry, agriculture, and other fields, though it easily leaks and is difficult to detect. In this work, we designed and synthesized a naphthalimide‐based fluorescent probe, which is easy to prepare, stable, and able to discriminate between phosgene, acetyl chloride, oxalyl chloride, thionyl chloride, phosphorus oxychloride, and tosyl chloride. Our results indicate that the probe can react with phosgene selectively and sensitively, showing remarkable ratiometric fluorescence changes. Furthermore, the probe can be made into test strips, which can determine phosgene in air effectively. The present work provides a novel class of naphthalimide‐based derivatives with potential application in phosgene sensing in real time simply and safely with further optimization.

Hydrazine is a highly toxic and flammable liquid that can damage human liver, kidney, and central nervous system. Therefore, it is valuable to seek a quick and sensitive method for hydrazine detection in environmental and biological science. Herein, a new fluorescent probe derived from 3-hydroxyphthalimide was synthesized. This probe can rapidly and selectively detect hydrazine with a low detection limit of 4.3 × 10 −7 M. The recognition principle is based on hydrazine-induced acetyl deprotection and excited-state intramolecular proton transfer (ESIPT) process. Moreover, test paper and fluorescence image experiments showed that this probe had potential to monitor hydrazine in the environment and living cells.

No abstract

No abstract

The question of how peptide chain aggregation is influenced by lipid membranes with varying shapes and structures is crucial for a detailed understanding of the neurotoxicity effect of the peptide chains. Not like the more usual spherical liposomes and planar lipid membranes, herein, we use lipid nanotubules as a model of important neuron synapse nanowire structures and devote particular attention to the effect of nanotubule fluidity on amyloid-β peptide (Aβ) chain aggregation. We apply single-molecule tracking (SMT) to elucidate how Aβ chains diffuse and aggregate on lipid nanotubules with different fluidities. The physical mechanism implies that fluidic lipid nanotubules facilitate the super-diffusion of two-dimensional (2D)-mobile precursor Aβ chains and promote their aggregation. This aggregation mechanism is retarded on less fluidic lipid nanotubules where the super-diffusion of 2D-mobile precursor Aβ chains is restricted by “frozen” lipids with less mobility. This work provides a mechanistic explanation for Aβ chain aggregation on fluidic lipid nanotubules.