Design of an artificial four-helix bundle metalloprotein via a novel ruthenium(II)-assisted self-assembly process

1992 ◽  
Vol 114 (10) ◽  
pp. 4000-4002 ◽  
Author(s):  
M. Reza Ghadiri ◽  
Christopher Soares ◽  
Chong Choi
2009 ◽  
Vol 48 (15) ◽  
pp. 2749-2751 ◽  
Author(s):  
Brooke A. Rosenzweig ◽  
Andrew D. Hamilton

Biochemistry ◽  
2000 ◽  
Vol 39 (36) ◽  
pp. 11041-11049 ◽  
Author(s):  
Brian R. Gibney ◽  
Yasuhiro Isogai ◽  
Francesc Rabanal ◽  
Konda S. Reddy ◽  
Anne M. Grosset ◽  
...  

2009 ◽  
Vol 121 (15) ◽  
pp. 2787-2789 ◽  
Author(s):  
Brooke A. Rosenzweig ◽  
Andrew D. Hamilton

2012 ◽  
Vol 13 (5) ◽  
pp. 1244-1249 ◽  
Author(s):  
Andrew F. Mehl ◽  
Stefan P. Feer ◽  
John S. Cusimano

Author(s):  
Krishna Sailaja A ◽  
Amareshwar P

In order to see the functionality and toxicity of nanoparticles in various food and drug applications, it is important to establish procedures to prepare nanoparticles of a controlled size. Desolvation is a thermodynamically driven self-assembly process for polymeric materials. In this study, we prepared BSA nanoparticles using the desolvation technique using acetone as desolvating agent. Acetone was added intermittently into 1% BSA solution at different pH under stirring at 700 rpm. Amount of acetone added, intermittent timeline of acetone addition, and pH of solution were considered as process parameters to be optimized. The effect of the process parameters on size of the nanoparticles was studied. The results indicated that the size control of BSA nanoparticles was achieved by adding acetone intermittently. The standard deviation of average size of BSA nanoparticles at each preparation condition was minimized by adding acetone intermittently. The intermittent addition in polymeric aqueous solution can be useful for size control for food or drug applications.  


Materials ◽  
2021 ◽  
Vol 14 (15) ◽  
pp. 4239
Author(s):  
Pezhman Mohammadi ◽  
Fabian Zemke ◽  
Wolfgang Wagermaier ◽  
Markus B. Linder

Macromolecular assembly into complex morphologies and architectural shapes is an area of fundamental research and technological innovation. In this work, we investigate the self-assembly process of recombinantly produced protein inspired by spider silk (spidroin). To elucidate the first steps of the assembly process, we examined highly concentrated and viscous pendant droplets of this protein in air. We show how the protein self-assembles and crystallizes at the water–air interface into a relatively thick and highly elastic skin. Using time-resolved in situ synchrotron X-ray scattering measurements during the drying process, we showed that the skin evolved to contain a high β-sheet amount over time. We also found that β-sheet formation strongly depended on protein concentration and relative humidity. These had a strong influence not only on the amount, but also on the ordering of these structures during the β-sheet formation process. We also showed how the skin around pendant droplets can serve as a reservoir for attaining liquid–liquid phase separation and coacervation from the dilute protein solution. Essentially, this study shows a new assembly route which could be optimized for the synthesis of new materials from a dilute protein solution and determine the properties of the final products.


Molecules ◽  
2021 ◽  
Vol 26 (12) ◽  
pp. 3598
Author(s):  
Nirmal K. Shee ◽  
Hee-Joon Kim

A series of porphyrin triads (1–6), based on the reaction of trans-dihydroxo-[5,15-bis(3-pyridyl)-10,20-bis(phenyl)porphyrinato]tin(IV) (SnP) with six different phenoxy Zn(II)-porphyrins (ZnLn), was synthesized. The cooperative metal–ligand coordination of 3-pyridyl nitrogens in the SnP with the phenoxy Zn(II)-porphyrins, followed by the self-assembly process, leads to the formation of nanostructures. The red-shifts and remarkable broadening of the absorption bands in the UV–vis spectra for the triads in CHCl3 indicate that nanoaggregates may be produced in the self-assembly process of these triads. The emission intensities of the triads were also significantly reduced due to the aggregation. Microscopic analyses of the nanostructures of the triads reveal differences due to the different substituents on the axial Zn(II)-porphyrin moieties. All these nanomaterials exhibited efficient photocatalytic performances in the degradation of rhodamine B (RhB) dye under visible light irradiation, and the degradation efficiencies of RhB in aqueous solution were observed to be 72~95% within 4 h. In addition, the efficiency of the catalyst was not impaired, showing excellent recyclability even after being applied for the degradation of RhB in up to five cycles.


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Shin Irumagawa ◽  
Kaito Kobayashi ◽  
Yutaka Saito ◽  
Takeshi Miyata ◽  
Mitsuo Umetsu ◽  
...  

AbstractThe stability of proteins is an important factor for industrial and medical applications. Improving protein stability is one of the main subjects in protein engineering. In a previous study, we improved the stability of a four-helix bundle dimeric de novo protein (WA20) by five mutations. The stabilised mutant (H26L/G28S/N34L/V71L/E78L, SUWA) showed an extremely high denaturation midpoint temperature (Tm). Although SUWA is a remarkably hyperstable protein, in protein design and engineering, it is an attractive challenge to rationally explore more stable mutants. In this study, we predicted stabilising mutations of WA20 by in silico saturation mutagenesis and molecular dynamics simulation, and experimentally confirmed three stabilising mutations of WA20 (N22A, N22E, and H86K). The stability of a double mutant (N22A/H86K, rationally optimised WA20, ROWA) was greatly improved compared with WA20 (ΔTm = 10.6 °C). The model structures suggested that N22A enhances the stability of the α-helices and N22E and H86K contribute to salt-bridge formation for protein stabilisation. These mutations were also added to SUWA and improved its Tm. Remarkably, the most stable mutant of SUWA (N22E/H86K, rationally optimised SUWA, ROSA) showed the highest Tm (129.0 °C). These new thermostable mutants will be useful as a component of protein nanobuilding blocks to construct supramolecular protein complexes.


Nanomaterials ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 1686
Author(s):  
Ruohong Sui ◽  
Paul A. Charpentier ◽  
Robert A. Marriott

In the past two decades, we have learned a great deal about self-assembly of dendritic metal oxide structures, partially inspired by the nanostructures mimicking the aesthetic hierarchical structures of ferns and corals. The self-assembly process involves either anisotropic polycondensation or molecular recognition mechanisms. The major driving force for research in this field is due to the wide variety of applications in addition to the unique structures and properties of these dendritic nanostructures. Our purpose of this minireview is twofold: (1) to showcase what we have learned so far about how the self-assembly process occurs; and (2) to encourage people to use this type of material for drug delivery, renewable energy conversion and storage, biomaterials, and electronic noses.


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