self assembly
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2022 ◽  
Vol 23 ◽  
pp. 100680
Qingyi Hu ◽  
Kejun Dong ◽  
Jie Ming ◽  
Wen Yang ◽  
Hongbo Wang ◽  

2022 ◽  
Vol 579 ◽  
pp. 152080
Alsu G. Nugmanova ◽  
Evgeniya A. Safonova ◽  
Alexander E. Baranchikov ◽  
Alexey R. Tameev ◽  
Andrey V. Shkolin ◽  

2022 ◽  
Vol 203 ◽  
pp. 111130
Deyin Wang ◽  
Xiaohui Wen ◽  
Dong Zhang ◽  
Aihua Chai

2022 ◽  
Vol 375 ◽  
pp. 115850
N.S. Saetova ◽  
A.A. Raskovalov ◽  
D.A. Kraynova ◽  
M.I. Vlasov ◽  
E.A. Il'ina ◽  

2022 ◽  
Gaurav Kumar ◽  
Sharmistha Sinha

Bacterial microcompartments are substrate specific metabolic modules that are conditionally expressed in certain bacterial species. These all protein structures have size in the range of 100-150 nm and are formed by the self-assembly of thousands of protein subunits, all encoded by genes belonging to a single operon. The operon contains genes that encode for both enzymes and shell proteins. The shell proteins self-assemble to form the outer coat of the compartment and enzymes are encapsulated within. A perplexing question in MCP biology is to understand the mechanism which governs the formation of these small yet complex assemblages of proteins. In this work we use 1,2-propanediol utilization microcompartments (PduMCP) as a paradigm to identify the factors that drive the self-assembly of MCP proteins. We find that a major shell protein PduBB tend to self-assemble under macromolecular crowded environment and suitable ionic strength. Microscopic visualization and biophysical studies reveal phase separation to be the principle mechanism behind the self-association of shell protein in the presence of salts and macromolecular crowding. The shell protein PduBB interacts with the enzyme diol-dehydratase PduCDE and co-assemble into phase separated liquid droplets. The co-assembly of PduCDE and PduBB results in the enhancement of catalytic activity of the enzyme. A combination of spectroscopic and biochemical techniques shows the relevance of divalent cation Mg2+ in providing stability to intact PduMCP in vivo. Together our results suggest a combination of protein-protein interactions and phase separation guiding the self-assembly of Pdu shell protein and enzyme in solution phase.

Coatings ◽  
2022 ◽  
Vol 12 (1) ◽  
pp. 97
Olga Bochkova ◽  
Alexey Dovjenko ◽  
Rustem Zairov ◽  
Kirill Kholin ◽  
Rinata Biktimirova ◽  

The present work introduces coordinative binding of CuII ions with both amino-functionalized silica nanoparticles (SNs) and green-emitting carbon dots (CDs) as the pregrequisite for the CuII-assisted self-assembly of the CDs at the surface of the SNs. The produced composite SNs exhibit stable in time stimuli-responsive green fluorescence derived from the CuII-assisted assemblage of CDs. The fluorescence response of the composite SNs is sensitive to the complex formation with glutathione (GSH), enabling them to detect it with the lower limit of detection of 0.15 μM. The spin-trap-facilitated electron spin resonance technique indicated that the composite SNs are capable of self-boosting generation of ROS due to CuII→CuI reduction by carbon in low oxidation states as a part of the CDs. The intensity of the ESR signals is enhanced under the heating to 38 °C. The intensity is suppressed at the GSH concentration of 0.35 mM but is enhanced at 1.0 mM of glutathione, while it is suppressed once more at the highest intracellular concentration level of GSH (10 mM). These tendencies reveal the concentrations optimal for the scavenger or reductive potential of GSH. Flow cytometry and fluorescence and confocal microscopy methods revealed efficient cell internalization of SNs-NH2-CuII-CDs comparable with that of “free” CDs.

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