Effect of Temperature and Humidity on Coarsening Behavior of Au Nanoparticles Embedded in Liquid Crystalline Lipid Membrane

Langmuir ◽  
2012 ◽  
Vol 28 (30) ◽  
pp. 10980-10987 ◽  
Author(s):  
Seung Jae Lee ◽  
Hyeun Hwan An ◽  
Won Bae Han ◽  
Hee-Soo Kim ◽  
Chong S. Yoon
2013 ◽  
Vol 13 (9) ◽  
pp. 6150-6152
Author(s):  
Seung Jae Lee ◽  
Hyeun Hwan An ◽  
Won Bae Han ◽  
Hee-Soo Kim ◽  
Yongdeok Kim ◽  
...  

Membranes ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 192
Author(s):  
Kinga Burdach ◽  
Dagmara Tymecka ◽  
Aneta Urban ◽  
Robert Lasek ◽  
Dariusz Bartosik ◽  
...  

The increasing resistance of bacteria to available antibiotics has stimulated the search for new antimicrobial compounds with less specific mechanisms of action. These include the ability to disrupt the structure of the cell membrane, which in turn leads to its damage. In this context, amphiphilic lipopeptides belong to the class of the compounds which may fulfill this requirement. In this paper, we describe two linear analogues of battacin with modified acyl chains to tune the balance between the hydrophilic and hydrophobic portion of lipopeptides. We demonstrate that both compounds display antimicrobial activity with the lowest values of minimum inhibitory concentrations found for Gram-positive pathogens. Therefore, their mechanism of action was evaluated on a molecular level using model lipid films mimicking the membrane of Gram-positive bacteria. The surface pressure measurements revealed that both lipopeptides show ability to bind and incorporate into the lipid monolayers, resulting in decreased ordering of lipids and membrane fluidization. Atomic force microscopy (AFM) imaging demonstrated that the exposure of the model bilayers to lipopeptides leads to a transition from the ordered gel phase to disordered liquid crystalline phase. This observation was confirmed by attenuated total reflection Fourier-transform infrared spectroscopy (ATR-FTIR) results, which revealed that lipopeptide action causes a substantial increase in the average tilt angle of lipid acyl chains with respect to the surface normal to compensate for lipopeptide insertion into the membrane. Moreover, the peptide moieties in both molecules do not adopt any well-defined secondary structure upon binding with the lipid membrane. It was also observed that a small difference in the structure of a lipophilic chain, altering the balance between hydrophobic and hydrophilic portion of the molecules, results in different insertion depth of the active compounds.


AIHAJ ◽  
1987 ◽  
Vol 48 (7) ◽  
pp. 639-645 ◽  
Author(s):  
R. NIELSEN ◽  
A.R. GWOSDOW ◽  
L.G. BERGLUND ◽  
A.B. DuBOIS

2000 ◽  
Vol 45 (1) ◽  
pp. 43-46 ◽  
Author(s):  
Myung-Koo Kang ◽  
Jong-Keuk Park ◽  
Doh-Yeon Kim ◽  
Nong-Moon Hwang

2006 ◽  
Vol 65 (3) ◽  
pp. 606-628 ◽  
Author(s):  
Annop Suriyasomboon ◽  
Nils Lundeheim ◽  
Annop Kunavongkrit ◽  
Stig Einarsson

1955 ◽  
Vol 90 (2) ◽  
pp. 446-448 ◽  
Author(s):  
S. A. Mayyasi ◽  
J. M. Birkeland ◽  
M. C. Dodd

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