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250106s2025 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.4c03391
|2 doi
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|a pubmed24n1655.xml
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|a eng
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|a Noe, Melania M
|e verfasserin
|4 aut
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| 245 |
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|a Whey-Derived Antimicrobial Anionic Peptide Interaction with Model Membranes and Cells
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|c 2025
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|a Text
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|a ƒaComputermedien
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|a Date Revised 06.01.2025
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|a published: Print-Electronic
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|a Citation Status Publisher
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|a The present work focuses on one of the possible target mechanisms of action of the anionic antimicrobial peptide β-lg125-135 derived from trypsin hydrolysis of β-lactoglobulin. After confirmation of bactericidal activity against a pathogenic Gram(+) strain and demonstration of the innocuousness on a eukaryotic cell line, we investigated the interaction of β-lg125-135 with monolayers and bilayers of dpPC and dpPC:dpPG as model membranes of eukaryotic and bacterial membranes, respectively. In monolayers, compared to zwitterionic dpPC, in the negatively charged dpPC-dpPG, β-lg125-135 injected into the subphase penetrated up to higher surface pressures and showed greater extents of penetration with increasing concentration in the subphase. Additionally, the rate constants for β-lg125-135 adsorption and desorption were 1 order of magnitude higher, and the resultant thermodynamic association constant was 1 order of magnitude lower. In turn, the compression isotherms of monolayers prepared with the β-lg125-135 present in the mixture spread over the air-water interface, remained in the monolayer and showed positive deviations from ideality, a greater decrease in the surface compressibility modulus, and an increase in the surface potential of both interfaces, more pronounced on dpPC:dpPG. In SUVs, fluorescence anisotropy (FA) assays using DPH and TMA-DPM indicated that β-lg125-135 tended to disrupt the gel phase of dpPC bilayers. Conversely, in dpPC:dpPG, the peptide increased the FA of both probes. These results reflect a relatively high tendency of the β-lg125-135 to approach the negative interface, with a favorable electrostatic orientation but low stability and short residence time. Once inside the membrane, it stiffens dpPG-containing bilayers
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|a Journal Article
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|a Rodríguez, Jésica A
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Barredo Vacchelli, Gabriela R
|e verfasserin
|4 aut
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| 700 |
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|a Camperi, Silvia A
|e verfasserin
|4 aut
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|a Franchi, Anahí N
|e verfasserin
|4 aut
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|a Turina, Anahí V
|e verfasserin
|4 aut
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| 700 |
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|a Perillo, María A
|e verfasserin
|4 aut
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| 700 |
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|a Nolan, Verónica
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1999
|g (2025) vom: 05. Jan.
|w (DE-627)NLM098181009
|x 1520-5827
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|g year:2025
|g day:05
|g month:01
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|u http://dx.doi.org/10.1021/acs.langmuir.4c03391
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