2011
DOI: 10.5539/ijc.v3n1p166
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Effect of Gramicidin D on the Compressibility and Volume Fluctuations of DPPC – Peptide Bilayers: A Densitometry and Sound Velocimetry Study

Abstract: The effects of increasing gramicidin D (gD) concentration on the partial specific volume, v o , and the adiabatic compressibility coefficient of the lipid, β S lipid of the bilayer reveals a continual decrease in  o and β S lipid (within the range of concentration studied) with concentration, except between 5 and 7.5 %, where a very slight decrease was observed. At gD concentrations higher than 5 mol%, the isothermal compressibility coefficient, β T lipid is greater than β S lipid at the gel-fluid region by … Show more

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Cited by 5 publications
(10 citation statements)
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“…Gramicidin has a low solubility in water (≤ 1 × 10 −4 μM according to Hladky and Haydon [32]) and has been found to partition strongly into the hydrophobic region of lipid membranes [33]. Hence, at the 0.1 μM gramicidin concentration adopted herein, much higher than its solubility value in pure water, it is quite reasonable for its concentration in the lipid bilayer to assume a value close to the 1:10 peptide/lipid molar ratio adopted in a theoretical analysis of hydrophobic matching [34], in a densitometry and sound velocimetry study on the effect of gramicidin [35], and in a STM imaging of gramicidin in a dimyristoylphosphatidylcholine (DMPC) monolayer on Au [36]. In particular, the counting of the lipid molecules surrounding each gramicidin channel yields an average number of 7 ± 1 [36], which is consistent with molecular dynamics calculations that assume eight nearestneighbor lipids [37].…”
Section: A Comparison With Experimental Cyclic Voltammogramsmentioning
confidence: 96%
“…Gramicidin has a low solubility in water (≤ 1 × 10 −4 μM according to Hladky and Haydon [32]) and has been found to partition strongly into the hydrophobic region of lipid membranes [33]. Hence, at the 0.1 μM gramicidin concentration adopted herein, much higher than its solubility value in pure water, it is quite reasonable for its concentration in the lipid bilayer to assume a value close to the 1:10 peptide/lipid molar ratio adopted in a theoretical analysis of hydrophobic matching [34], in a densitometry and sound velocimetry study on the effect of gramicidin [35], and in a STM imaging of gramicidin in a dimyristoylphosphatidylcholine (DMPC) monolayer on Au [36]. In particular, the counting of the lipid molecules surrounding each gramicidin channel yields an average number of 7 ± 1 [36], which is consistent with molecular dynamics calculations that assume eight nearestneighbor lipids [37].…”
Section: A Comparison With Experimental Cyclic Voltammogramsmentioning
confidence: 96%
“…This antimicrobial peptide is in fact a mixture of pore forming peptides (gramicidin A 80%, B 6% and C 14%), 156 called collectively gramicidin D. 35 Gramicidin D has a linear chain made of 15 amino acids, 157 as opposed to gramicidin S that forms a cyclic peptide chain. 158 Alamethicin is another channelforming peptide antibiotic, that can induce voltage-dependent ion channels in lipid membranes. 159 Despite being made of only 20 amino acids, alamethicin exhibits channeling activity that is suggested to be relevant to that of physiological channel proteins which typically consist of 2,000 or more amino acids.…”
Section: Peptidesmentioning
confidence: 99%
“…35 These pore forming peptides have also been acting as model systems in various studies 17,[153][154][155] aiming at evaluating the changes of membrane electrical properties upon insertion of peptides 35 . These peptides are produced by soil bacterial species Bacillus brevis and are active against Gram-positive bacteria except for the Gram-positive bacilli against selected Gram-negative organisms, such as Neisseria bacteria 158 . Gramicidin D has a linear chain made of 15 amino acids 157 , opposed to gramicidin S that forms a cyclic peptide chain 158 .…”
Section: Transmembrane Peptides: Gramicidin Alamethicin and Melittinmentioning
confidence: 99%
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