Modeling of an origami robot driven by electrostatic forces

Author(s):  
Jisen Li ◽  
Hareesh Godaba ◽  
Zhiqian Zhang ◽  
Choon Chiang Foo ◽  
Jian Zhu
Keyword(s):  
2000 ◽  
Vol 10 (1-2) ◽  
pp. 15
Author(s):  
Eugene Sprague ◽  
Julio C. Palmaz ◽  
Cristina Simon ◽  
Aaron Watson

Molecules ◽  
2021 ◽  
Vol 26 (8) ◽  
pp. 2363
Author(s):  
Darya A. Kuznetsova ◽  
Dinar R. Gabdrakhmanov ◽  
Denis M. Kuznetsov ◽  
Svetlana S. Lukashenko ◽  
Valery M. Zakharov ◽  
...  

The solution behavior and physicochemical characteristics of polymer–colloid complexes based on cationic imidazolium amphiphile with a dodecyl tail (IA-12) and polyacrylic acid (PAA) or DNA decamer (oligonucleotide) were evaluated using tensiometry, conductometry, dynamic and electrophoretic light scattering and fluorescent spectroscopy and microscopy. It has been established that PAA addition to the surfactant system resulted in a ca. 200-fold decrease in the aggregation threshold of IA-12, with the hydrodynamic diameter of complexes ranging within 100–150 nm. Electrostatic forces are assumed to be the main driving force in the formation of IA-12/PAA complexes. Factors influencing the efficacy of the complexation of IA-12 with oligonucleotide were determined. The nonconventional mode of binding with the involvement of hydrophobic interactions and the intercalation mechanism is probably responsible for the IA-12/oligonucleotide complexation, and a minor contribution of electrostatic forces occurred. The latter was supported by zeta potential measurements and the gel electrophoresis technique, which demonstrated the low degree of charge neutralization of the complexes. Importantly, cellular uptake of the IA-12/oligonucleotide complex was confirmed by fluorescence microscopy and flow cytometry data on the example of M-HeLa cells. While single IA-12 samples exhibit roughly similar cytotoxicity, IA-12–oligonucleotide complexes show a selective effect toward M-HeLa cells (IC50 1.1 µM) compared to Chang liver cells (IC50 23.1 µM).


2019 ◽  
Vol 56 (6) ◽  
pp. 1680-1688
Author(s):  
Joseph Hughes ◽  
Hanspeter Schaub

1985 ◽  
Vol 230 (1) ◽  
pp. 277-280 ◽  
Author(s):  
K Gietzen ◽  
H J Galla

Seminalplasmin, a strongly basic protein isolated from bull semen, was found to antagonize with high potency and extraordinary specificity the function of calmodulin. Calmodulin antagonism is the result of an interaction between the two proteins, which is mainly determined by electrostatic forces. The stimulation of Ca2+-transporting ATPase and phosphodiesterase by calmodulin was half-maximally inhibited at approx. 0.1 microM-seminalplasmin. However, the basal activity of calmodulin-dependent enzymes was not significantly altered by seminalplasmin over the concentration range investigated.


Author(s):  
Nadine Aubry ◽  
Pushpendra Singh

The objective of this paper is to study the dependence of the electrostatic force that act on a particle within the interface between two immiscible fluids on the parameters such as the dielectric properties of the fluids and particles, the particle’s position within the interface, and the electric field strength. It is shown that the component of electrostatic force normal to the interface varies as a2, where a is the particle radius, and since in equilibrium it is balanced by the vertical capillary force, the interfacial deformation caused by the particle changes when an external electric field is applied. In addition, there are lateral electrostatic forces among the particles due to the dipole-dipole interactions which, when the distance between two particles is O(a), vary as a2, and remain significant for submicron sized particles.


1995 ◽  
Vol 77 (7) ◽  
pp. 3308-3314 ◽  
Author(s):  
S. Hudlet ◽  
M. Saint Jean ◽  
B. Roulet ◽  
J. Berger ◽  
C. Guthmann

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