Divalent cations modulate membrane binding and pore formation of a potent antibiotic peptide analog of alamethicin

Cell Calcium ◽  
2013 ◽  
Vol 53 (3) ◽  
pp. 180-186 ◽  
Author(s):  
Marco Aquila ◽  
Mascia Benedusi ◽  
Karl-Wilhelm Koch ◽  
Daniele Dell’Orco ◽  
Giorgio Rispoli
Keyword(s):  
Pore Formation ◽  
Divalent Cations ◽  
Membrane Binding ◽  
Peptide Analog ◽  
Antibiotic Peptide

scholarly journals Dual modes of membrane binding direct pore formation by Streptolysin O

2015 ◽  
Vol 97 (6) ◽  
pp. 1036-1050 ◽  
Author(s):  
Cara C. Mozola ◽  
Michael G. Caparon
Keyword(s):  
Pore Formation ◽  
Membrane Binding ◽  
Streptolysin O

The structural basis for membrane binding and pore formation by lymphocyte perforin

Nature ◽  
2010 ◽  
Vol 468 (7322) ◽  
pp. 447-451 ◽  
Author(s):  
Ruby H. P. Law ◽  
Natalya Lukoyanova ◽  
Ilia Voskoboinik ◽  
Tom T. Caradoc-Davies ◽  
Katherine Baran ◽  
...  
Keyword(s):  
Pore Formation ◽  
Membrane Binding ◽  
Structural Basis

scholarly journals Bax-type Apoptotic Proteins Porate Pure Lipid Bilayers through a Mechanism Sensitive to Intrinsic Monolayer Curvature

2002 ◽  
Vol 277 (51) ◽  
pp. 49360-49365 ◽  
Author(s):  
Gorka Basañez ◽  
Juanita C. Sharpe ◽  
Jennifer Galanis ◽  
Teresa B. Brandt ◽  
J. Marie Hardwick ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Mitochondrial Membrane ◽  
Pore Formation ◽  
Membrane Binding ◽  
Membrane Permeabilization ◽  
Outer Mitochondrial Membrane ◽  
Intrinsic Curvature ◽  
Differential Effects ◽  
Cleavage Fragment ◽  
Induced Changes

During apoptosis, Bax-type proteins permeabilize the outer mitochondrial membrane to release intermembrane apoptogenic factors into the cytosol via a poorly understood mechanism. We have proposed that Bax and ΔN76Bcl-xL(the Bax-like cleavage fragment of Bcl-xL) function by forming pores that are at least partially composed of lipids (lipidic pore formation). Since the membrane monolayer must bend during lipidic pore formation, we here explore the effect of intrinsic membrane monolayer curvature on pore formation. Nonlamellar lipids with positive intrinsic curvature such as lysophospholipids promoted membrane permeabilization, whereas nonlamellar lipids with negative intrinsic curvature such as diacylglycerol and phosphatidylethanolamine inhibited membrane permeabilization. The differential effects of nonlamellar lipids on membrane permeabilization were not correlated with lipid-induced changes in membrane binding or insertion of Bax or ΔN76Bcl-xL. Altogether, these results are consistent with a model whereby Bax-type proteins change the bending propensity of the membrane to form pores comprised at least in part of lipids in a structure of net positive monolayer curvature.

Effect of Divalent Cations on Pore Formation and Degradation of Poly(D,L-lactide-co-glycolide)

2007 ◽  
Vol 12 (6) ◽  
pp. 563-572 ◽  
Author(s):  
Susanne Fredenberg ◽  
Mats Reslow ◽  
Anders Axelsson
Keyword(s):  
Pore Formation ◽  
Divalent Cations

Membrane Binding and Pore Formation by a Cytotoxic Fragment of Amyloid β Peptide

2017 ◽  
Vol 121 (45) ◽  
pp. 10293-10305 ◽  
Author(s):  
Nabin Kandel ◽  
Tianyu Zheng ◽  
Qun Huo ◽  
Suren A. Tatulian
Keyword(s):  
Pore Formation ◽  
Membrane Binding ◽  
Amyloid Β ◽  
Amyloid Β Peptide

scholarly journals Lipid II-Mediated Pore Formation by the Peptide Antibiotic Nisin: a Black Lipid Membrane Study

2004 ◽  
Vol 186 (10) ◽  
pp. 3259-3261 ◽  
Author(s):  
Imke Wiedemann ◽  
Roland Benz ◽  
Hans-Georg Sahl
Keyword(s):  
Cell Wall ◽  
Pore Formation ◽  
Cytoplasmic Membrane ◽  
Lipid Membrane ◽  
Specific Interaction ◽  
Peptide Antibiotic ◽  
Black Lipid Membrane ◽  
Lipid Ii ◽  
Antibiotic Peptide

ABSTRACT The antibiotic peptide nisin is the first known lantibiotic that uses a docking molecule within the bacterial cytoplasmic membrane for pore formation. Through specific interaction with the cell wall precursor lipid II, nisin forms defined pores which are stable for seconds and have pore diameters of 2 to 2.5 nm.

Membrane Binding and Pore Formation of the Antibacterial Peptide PGLa:  Thermodynamic and Mechanistic Aspects†

Biochemistry ◽  
2000 ◽  
Vol 39 (2) ◽  
pp. 442-452 ◽  
Author(s):  
Torsten Wieprecht ◽  
Ognjan Apostolov ◽  
Michael Beyermann ◽  
Joachim Seelig
Keyword(s):  
Pore Formation ◽  
Membrane Binding ◽  
Antibacterial Peptide

Common action of certain viruses, toxins, and activated complement: pore formation and its prevention by extracellular Ca2+

1984 ◽  
Vol 4 (9) ◽  
pp. 797-805 ◽  
Author(s):  
C. L. Bashford ◽  
G. M. Alder ◽  
K. Patel ◽  
C. A. Pasternak
Keyword(s):  
Membrane Potential ◽  
Pore Formation ◽  
Divalent Cations ◽  
Surface Membrane ◽  
Daudi Cells ◽  
High Concentrations ◽  
Common Action

Haemolysis by Sendal virus, α-toxin, and activated complement is inhibited by high concentrations of divalent cations. In Daudi cells, sublytic amounts of these agents induce the following changes: collapse of surface membrane potential, uptake of Na+ and loss of K+ from cells, and leakage of phosphorylated metabo-tites from cells. The changes induced by Sendal virus and complement are sensitive to physiological concentrations of extracellular Ca2+. It is concluded that fluctuations in plasma Ca2+ concentration may affect the damaging action of certain pore-forming agents on susceptible cells.

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