scholarly journals Exploring the self-assembly and energy transfer of dynamic supramolecular iridium-porphyrin systems

2016 ◽  
Vol 45 (43) ◽  
pp. 17195-17205 ◽  
Author(s):  
Diego Rota Martir ◽  
Gordon J. Hedley ◽  
David B. Cordes ◽  
Alexandra M. Z. Slawin ◽  
Daniel Escudero ◽  
...  

We present the first examples of dynamic supramolecular iridium–zinc porphyrin systems.

2013 ◽  
Vol 575-576 ◽  
pp. 123-129
Author(s):  
Zhuang Dong Yuan ◽  
Jing Xia Wang ◽  
Ning Sheng

DABCO (1, 4-diazabicyclo [2.2.2] octane) has been used in combination with pentameric zinc porphyrin-pyrene array 1 to form well-defined supramolecular arrays through axial coordination. The self-assembly process has been investigated by a wide range of spectroscopic methods including UV-vis, fluorescence emission and 1H NMR techniques.


2010 ◽  
Vol 16 (17) ◽  
pp. 5052-5061 ◽  
Author(s):  
Chihiro Maeda ◽  
Pyosang Kim ◽  
Sung Cho ◽  
Jong Kang Park ◽  
Jong Min Lim ◽  
...  

Biosensors ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 505
Author(s):  
Guangze Yang ◽  
Yun Liu ◽  
Jisi Teng ◽  
Chun-Xia Zhao

Fluorescence labelling is often used for tracking nanoparticles, providing a convenient assay for monitoring nanoparticle drug delivery. However, it is difficult to be quantitative, as many factors affect the fluorescence intensity. Förster resonance energy transfer (FRET), taking advantage of the energy transfer from a donor fluorophore to an acceptor fluorophore, provides a distance ruler to probe NP drug delivery. This article provides a review of different FRET approaches for the ratiometric monitoring of the self-assembly and formation of nanoparticles, their in vivo fate, integrity and drug release. We anticipate that the fundamental understanding gained from these ratiometric studies will offer new insights into the design of new nanoparticles with improved and better-controlled properties.


2018 ◽  
Vol 6 (10) ◽  
pp. 2452-2459 ◽  
Author(s):  
Nathaniel T. Anderson ◽  
Peter H. Dinolfo ◽  
Xing Wang

A new type of modular energy transfer system has been synthesized using ssDNA and a porphyrin molecule through CuAAC reactivity.


2015 ◽  
Vol 17 (31) ◽  
pp. 20322-20330 ◽  
Author(s):  
Sijing Yi ◽  
Jiao Wang ◽  
Xiao Chen

The self-assembly of luminescent lyotropic liquid crystals with europium β-diketonate complex confined within via hydrogen bonds between P123 and imidazolium cations is demonstrated.


Author(s):  
M. Kessel ◽  
R. MacColl

The major protein of the blue-green algae is the biliprotein, C-phycocyanin (Amax = 620 nm), which is presumed to exist in the cell in the form of distinct aggregates called phycobilisomes. The self-assembly of C-phycocyanin from monomer to hexamer has been extensively studied, but the proposed next step in the assembly of a phycobilisome, the formation of 19s subunits, is completely unknown. We have used electron microscopy and analytical ultracentrifugation in combination with a method for rapid and gentle extraction of phycocyanin to study its subunit structure and assembly.To establish the existence of phycobilisomes, cells of P. boryanum in the log phase of growth, growing at a light intensity of 200 foot candles, were fixed in 2% glutaraldehyde in 0.1M cacodylate buffer, pH 7.0, for 3 hours at 4°C. The cells were post-fixed in 1% OsO4 in the same buffer overnight. Material was stained for 1 hour in uranyl acetate (1%), dehydrated and embedded in araldite and examined in thin sections.


Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.


MRS Advances ◽  
2020 ◽  
Vol 5 (64) ◽  
pp. 3507-3520
Author(s):  
Chunhui Dai ◽  
Kriti Agarwal ◽  
Jeong-Hyun Cho

AbstractNanoscale self-assembly, as a technique to transform two-dimensional (2D) planar patterns into three-dimensional (3D) nanoscale architectures, has achieved tremendous success in the past decade. However, an assembly process at nanoscale is easily affected by small unavoidable variations in sample conditions and reaction environment, resulting in a low yield. Recently, in-situ monitored self-assembly based on ion and electron irradiation has stood out as a promising candidate to overcome this limitation. The usage of ion and electron beam allows stress generation and real-time observation simultaneously, which significantly enhances the controllability of self-assembly. This enables the realization of various complex 3D nanostructures with a high yield. The additional dimension of the self-assembled 3D nanostructures opens the possibility to explore novel properties that cannot be demonstrated in 2D planar patterns. Here, we present a rapid review on the recent achievements and challenges in nanoscale self-assembly using electron and ion beam techniques, followed by a discussion of the novel optical properties achieved in the self-assembled 3D nanostructures.


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