Insight into the Aggregation Prospective of Schiff Base AIEgens Enabling Efficient Hydrazine Sensor in their Aggregated State

Author(s):  
Senjuti Halder ◽  
Biswajit Nayak ◽  
Basu Bhattacharjee ◽  
Ramesh Aiyagari ◽  
Gopal Das

In this study, we present two small fluorogenic Schiff base molecules 1 and 2 encompassing both donor and acceptor moiety in the single-molecule to trigger the AIE activity and report...

CrystEngComm ◽  
2021 ◽  
Author(s):  
Mainak Karmakar ◽  
Antonio Frontera ◽  
Shouvik Chattopadhyay

The formation of an infinite 1D assembly is governed by the H-bonding interactions in the solid state structure of the two zinc complexes. It has been analyzed energetically using DFT calculations and several computational tools.


2015 ◽  
Vol 44 (29) ◽  
pp. 13242-13249 ◽  
Author(s):  
Malay Dolai ◽  
Mahammad Ali ◽  
Ján Titiš ◽  
Roman Boča

Two CuII–DyIII and CoIII–DyIII dinuclear complexes of a Schiff base ligand (H3L) exhibit single-molecule magnetic behaviour with multiple slow magnetic relaxation processes for the former.


2012 ◽  
Vol 610-613 ◽  
pp. 3574-3579
Author(s):  
Cui Hua Wang ◽  
Sheng Long Yang ◽  
Chao Lu ◽  
Hong Xia Yu ◽  
Lian Shen Wang ◽  
...  

By using CoMFA and CoMSIA methods, the new quantitative structures of 25 aromatic hydrocarbons and the 96 hr-EC50 data with C. vulgaris have been investigated to obtain more detailed insight into the relationships between molecular structure and bioactivity. Compared to CoMFA (the average Q2LOO option =0.610), CoMSIA (the average Q2LOO =0.736) has the better results with robustness and stability. CoMSIA analysis using steric, electrostatic, hydrophobic, and H-bond donor and acceptor descriptors show H-bond donor is the common factor for influencing the toxicity, the steric and electrostatic descriptors are next and the hydrophobic descriptor was last. From the contour maps, the number of benzene ring is more crucial for the compound toxicity and the compounds with more benzene ring make toxicity increased. Under the same number of benzene ring, the kind of substituent group and the formed ability of H-bond are the other parameters to influencing the aromatic hydrocarbons toxicity.


2016 ◽  
Vol 45 (8) ◽  
pp. 3616-3626 ◽  
Author(s):  
Apoorva Upadhyay ◽  
Chinmoy Das ◽  
Stuart K. Langley ◽  
Keith S. Murray ◽  
Anant K. Srivastava ◽  
...  

The crystal structures are reported for three heterometallic Ni2Ln and a Ni2Dy2 complex, using the Schiff base ligand 2-methoxy-6-[(E)-phenyliminomethyl] phenol. Detailed dc and ac magnetic susceptibility studies were reported for all the complexes. The complexes 3 and 4 shows frequency dependent out-of-phase susceptibility signals.


2016 ◽  
Vol 18 (4) ◽  
pp. 2730-2735 ◽  
Author(s):  
Qiang Sun ◽  
Liangliang Cai ◽  
Yuanqi Ding ◽  
Honghong Ma ◽  
Chunxue Yuan ◽  
...  

We have performed a systematic study of Wurtz reactions on different metal surfaces and compared their different activities.


Author(s):  
Ilina Bareja ◽  
Hugo Wioland ◽  
Miro Janco ◽  
Philip R. Nicovich ◽  
Antoine Jégou ◽  
...  

ABSTRACTTropomyosins regulate dynamics and functions of the actin cytoskeleton by forming long chains along the two strands of actin filaments that act as gatekeepers for the binding of other actin-binding proteins. The fundamental molecular interactions underlying the binding of tropomyosin to actin are still poorly understood. Using microfluidics and fluorescence microscopy, we observed the binding of fluorescently labelled tropomyosin isoform Tpm1.8 to unlabelled actin filaments in real time. This approach in conjunction with mathematical modeling enabled us to quantify the nucleation, assembly and disassembly kinetics of Tpm1.8 on single filaments and at the single molecule level. Our analysis suggests that Tpm1.8 decorates the two strands of the actin filament independently. Nucleation of a growing tropomyosin domain proceeds with high probability as soon as the first Tpm1.8 molecule is stabilised by the addition of a second molecule, ultimately leading to full decoration of the actin filament. In addition, Tpm1.8 domains are asymmetrical, with enhanced dynamics at the edge oriented towards the barbed end of the actin filament. The complete description of Tpm1.8 kinetics on actin filaments presented here provides molecular insight into actin-tropomyosin filament formation and the role of tropomyosins in regulating actin filament dynamics.


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