The aminosterol antibiotic squalamine permeabilizes large unilamellar phospholipid vesicles. (Q52530139)

2 May 2018

title

The aminosterol antibiotic squalamine permeabilizes large unilamellar phospholipid vesicles. (English)

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2 May 2018

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B S Selinsky

1

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2 May 2018

Z Zhou

2

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2 May 2018

K G Fojtik

3

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2 May 2018

S R Jones

4

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2 May 2018

N R Dollahon

5

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2 May 2018

A E Shinnar

6

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2 May 2018

publication date

1 March 1998

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2 May 2018

Biochimica et Biophysica Acta

number of pages

17

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based on heuristic

inferred from page(s)

published in

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2 May 2018

volume

1370

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2 May 2018

issue

2

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2 May 2018

page(s)

218-234

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2 May 2018

Antibacterial peptides: key components needed in immunity

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Small-volume extrusion apparatus for preparation of large, unilamellar vesicles

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Magainin 1-induced leakage of entrapped calcein out of negatively-charged lipid vesicles

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Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore

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Surfactant-induced release of liposomal contents. A survey of methods and results

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The influence of membrane composition on the solubilizing effects of Triton X-100

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Interaction of calcium and cholesterol sulphate induces membrane destabilization and fusion: implications for the acrosome reaction.

7 January 2021

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2'-(3 alpha-Benzyloxy-24-norcholan-23-yl)-2',4',4'-trimethyl-4',5'- dihydrooxazoline-N-oxyl as a potential spin probe for model membranes.

7 January 2021

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An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation.

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10.1016/S0005-2736(97)00265-4

7 January 2021

Identifiers

DOI

1 reference

2 May 2018

PubMed ID

9545568

1 reference

2 May 2018