scholarly journals Synthetic Multifunctional Nanoarchitecture in Lipid Bilayers: Ion Channels, Sensors, and Photosystems

2007 ◽  
Vol 80 (6) ◽  
pp. 1044-1057 ◽  
Author(s):  
Rajesh Bhosale ◽  
Sheshanath Bhosale ◽  
Guillaume Bollot ◽  
Virginie Gorteau ◽  
Marc D. Julliard ◽  
...  
Keyword(s):  
Ion Channels ◽  
Lipid Bilayers

scholarly journals Bright Ion Channels and Lipid Bilayers

2013 ◽  
Vol 46 (12) ◽  
pp. 2910-2923 ◽  
Author(s):  
Wiktor SzymaŃski ◽  
Duygu Yilmaz ◽  
ArmaĞan Koçer ◽  
Ben L. Feringa
Keyword(s):  
Ion Channels ◽  
Lipid Bilayers

Reconstitution of Single Potassium Channels from Bovine Gallbladder Epithelium

1998 ◽  
Vol 26 (4) ◽  
pp. 188-199
Author(s):  
E Kyriacou
Keyword(s):  
Ion Channels ◽  
Gall Bladder ◽  
Lipid Bilayers ◽  
Membrane Vesicle ◽  
Basolateral Membrane ◽  
Molecular Transport ◽  
Membrane Vesicles ◽  
Potassium Ion ◽  
Potassium Ion Channels ◽  
Adult Cattle

The study of molecular transport across gall-bladder epithelium may contribute to our understanding of the pathophysiology of gall-bladder disease. The aim of this study was to reconstitute and characterize single potassium ion channels in bovine gall-bladder epithelial mucosa – both apical and basolateral aspects. Standard subcellular fractionation techniques were used to form either apical or basolateral closed-membrane vesicles from the mucosal epithelium of fresh gall bladders from healthy young adult cattle. Vesicular ion channels were incorporated into voltage-clamped planar lipid bilayers under known ionic conditions and their conductances, reversal potentials, and voltages were characterized. Low-conductance voltage-insensitive apical membrane vesicle channels of at least four conductance levels were found (mean ± SD): 12 ± 4 pS, n = 10; 40 ± 12 pS, n = 4; 273 ± 31 pS, n = 3; and 151 ± 24 pS, n = 5. Conductances of potassium ion channels in basolateral membrane vesicles were in the range 9–450 pS, and these channels included high-conductance calcium-activated potassium-ion channels ‘K(Ca)’ which were voltage- and calcium-dependent.

scholarly journals All D-Amino Acids Amyloid β Forms Ion Channels in Lipid Bilayers and is Toxic to Cells

2012 ◽  
Vol 102 (3) ◽  
pp. 616a-617a
Author(s):  
Ricardo Capone ◽  
Hyunbum Jang ◽  
Samuel A. Kotler ◽  
Laura Connelly ◽  
Michael Williams ◽  
...  
Keyword(s):  
Amino Acids ◽  
Ion Channels ◽  
Lipid Bilayers ◽  
Amyloid Β

Ion-channel properties of mastoparan, a 14-residue peptide from wasp venom, and of MP3, a 12-residue analogue

1990 ◽  
Vol 239 (1296) ◽  
pp. 383-400 ◽  
Keyword(s):  
Ion Channels ◽  
Lipid Bilayers ◽  
Type I ◽  
Type Ii ◽  
Channel Formation ◽  
Channel Inactivation ◽  
Ion Channel Properties ◽  
Discrete Channel ◽  
Voltage Dependent ◽  
Channel Properties

Mastoparan, a 14-residue peptide, has been investigated with respect to its ability to form ion channels in planar lipid bilayers. In the presence of 0.3 - 3.0 μ M mastoparan, two types of activity are seen. Type I activity is characterized by discrete channel openings, exhibiting multiple con­ductance levels in the range 15-700 pS. Type II activity is characterized by transient increases in bilayer conductance, up to a maximum of about 650 pS. Both type I and type II activities are voltage dependent. Channel activation occurs if the compartment containing mastoparan is held at a positive potential; channel inactivation if the same compartment is held at a negative potential. Channel formation is dependent on ionic strength; channel openings are only observed at KCl concentrations of 0.3 M or above. Furthermore, raising the concentration of KCl to 3.0 M stabilizes the open form of the channel. Mastoparan channels are weakly cation selective, P K/Cl ≈ 2. A 12-residue analogue, des -Ile 1 , Asn 2 mastoparan, preferentially forms type I channels. The ion channels formed by these short peptides may be modelled in terms of bundles of transmembrane α -helices.

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