Triggered Interactions between Nanoparticles and Lipid Membranes: Design Principles for Gel Formation or Disruption-and-Release

Soft Matter ◽  
2021 ◽  
Author(s):  
Rui Cao ◽  
Jingjing Gao ◽  
Sankaran Thayumanavan ◽  
Anthony D. Dinsmore
Keyword(s):  
Lipid Bilayer ◽  
Lipid Membranes ◽  
Design Principles ◽  
Gel Formation ◽  
Synergistic Interactions ◽  
Lipid Bilayer Vesicles

Lipid bilayer vesicles offer exciting possibilities for stimulated response, taking advantage of the membrane’s flexibility and impermeability. We show how synergistic interactions between vesicles and polymer-based nanoparticles can be triggered...

Scaling analysis of narrow necks in curvature models of fluid lipid-bilayer vesicles

1994 ◽  
Vol 49 (6) ◽  
pp. 5276-5286 ◽  
Author(s):  
Bertrand Fourcade ◽  
Ling Miao ◽  
Madan Rao ◽  
Michael Wortis ◽  
R. K. P. Zia
Keyword(s):  
Lipid Bilayer ◽  
Scaling Analysis ◽  
Lipid Bilayer Vesicles

Budding of lipid bilayer vesicles and flat membranes

1992 ◽  
Vol 4 (7) ◽  
pp. 1647-1657 ◽  
Author(s):  
W Wiese ◽  
W Harbich ◽  
W Helfrich
Keyword(s):  
Lipid Bilayer ◽  
Lipid Bilayer Vesicles ◽  
Flat Membranes

scholarly journals Formation and properties of cell-size lipid bilayer vesicles

1983 ◽  
Vol 44 (3) ◽  
pp. 375-381 ◽  
Author(s):  
P. Mueller ◽  
T.F. Chien ◽  
B. Rudy
Keyword(s):  
Cell Size ◽  
Lipid Bilayer ◽  
Lipid Bilayer Vesicles

TRICONCAVE SOLUTION TO THE HELFRICH VARIATION PROBLEM FOR THE SHAPE OF LIPID BILAYER VESICLES IS FOUND BY "SURFACE EVOLVER"

2002 ◽  
Vol 16 (03) ◽  
pp. 511-517 ◽  
Author(s):  
YONG ZHANG ◽  
XIN ZHOU ◽  
JIANJUN ZHOU ◽  
ZHONG-CAN OU-YANG
Keyword(s):  
Blood Cell ◽  
Lipid Bilayer ◽  
Red Blood Cell ◽  
Physical Parameters ◽  
Spontaneous Curvature ◽  
Fresh Blood ◽  
Surface Evolver ◽  
Variation Problem ◽  
Lipid Bilayer Vesicles

We numerically show the existence of triconcave Red Blood Cell (RBC) according to Helfrich spontaneous curvature model. It suggests that the Helfrich spontaneous curvature model can well work in the case of non-axisymmetric vesicle. Some geometric and physical parameters are obtained to describe the triconcave RBC which has been observed in fresh blood under the circumstance of certain hemolytic anemias. Comparing with the normal RBC, we find that the differences between the interior and the exterior of the triconcave RBC are smaller than that of the normal RBC.

Pore Formation of Thermostable Direct Hemolysin Secreted from Vibrio parahaemolyticus in Lipid Bilayers

2006 ◽  
Vol 25 (5) ◽  
pp. 409-418 ◽  
Author(s):  
Akira Takahashi ◽  
Chiyo Yamamoto ◽  
Toshio Kodama ◽  
Kanami Yamashita ◽  
Nagakatsu Harada ◽  
...  
Keyword(s):  
Lipid Bilayer ◽  
Lipid Bilayers ◽  
Lipid Membranes ◽  
Vibrio Parahaemolyticus ◽  
Cultured Cells ◽  
Ion Selectivity ◽  
Ion Permeability ◽  
Lower Extent ◽  
Thermostable Direct Hemolysin ◽  
Mutant Toxin

Vibrio parahaemolyticus secretes thermostable direct hemolysin (TDH), a major virulence factor. Earlier studies report that TDH is a pore-forming toxin. However, the characteristics of pores formed by TDH in the lipid bilayer, which is permeable to small ions, remain to be elucidated. Ion channel-like activities were observed in lipid bilayers containing TDH. Three types of conductance were identified. All the channels displayed relatively low ion selectivity, and similar ion permeability. The Cl− channel inhibitors, DIDS, glybenclamide, and NPPB, did not affect the channel activity of pores formed by TDH. R7, a mutant toxin of TDH, also forms pores with channel-like activity in lipid bilayers. The ion permeability of these channels is similar to that of TDH. R7 binds cultured cells and liposomes to a lower extent, compared to TDH. R7 does not display significant hemolytic activity and cell cytotoxicity, possibly owing to the difficulty of insertion into lipid membranes. Once R7 is assembled within lipid membranes, it may assume the same structure as TDH. The authors propose that the single glycine at position 62, substituted with serine in the R7 mutant toxin, plays an important role in TDH insertion into the lipid bilayer.

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