Penetration of Milk-Derived Antimicrobial Peptides into Phospholipid Monolayers as Model Biomembranes

Three antimicrobial peptides derived from bovine milk proteins were examined with regard to penetration into insoluble monolayers formed with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) or 1,2-dipalmitoyl-sn-glycero-3-phospho-rac-(1-glycerol) sodium salt (DPPG). Effects on surface pressure (Π...

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Main Authors: Wanda Barzyk, Ewa Rogalska, Katarzyna Więcław-Czapla
Format: Article
Language:English
Published: Wiley 2013-01-01
Series:Biochemistry Research International
Online Access:http://dx.doi.org/10.1155/2013/914540
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author Wanda Barzyk
Ewa Rogalska
Katarzyna Więcław-Czapla
author_facet Wanda Barzyk
Ewa Rogalska
Katarzyna Więcław-Czapla
author_sort Wanda Barzyk
collection DOAJ
description Three antimicrobial peptides derived from bovine milk proteins were examined with regard to penetration into insoluble monolayers formed with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) or 1,2-dipalmitoyl-sn-glycero-3-phospho-rac-(1-glycerol) sodium salt (DPPG). Effects on surface pressure (Π) and electric surface potential (ΔV) were measured, Π with a platinum Wilhelmy plate and ΔV with a vibrating plate. The penetration measurements were performed under stationary diffusion conditions and upon the compression of the monolayers. The two type measurements showed greatly different effects of the peptide-lipid interactions. Results of the stationary penetration show that the peptide interactions with DPPC monolayer are weak, repulsive, and nonspecific while the interactions with DPPG monolayer are significant, attractive, and specific. These results are in accord with the fact that antimicrobial peptides disrupt bacteria membranes (negative) while no significant effect on the host membranes (neutral) is observed. No such discrimination was revealed from the compression isotherms. The latter indicate that squeezing the penetrant out of the monolayer upon compression does not allow for establishing the penetration equilibrium, so the monolayer remains supersaturated with the penetrant and shows an under-equilibrium orientation within the entire compression range, practically.
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issn 2090-2247
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publishDate 2013-01-01
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series Biochemistry Research International
spelling doaj-art-70bc0e919835464ea0f3ac96e07eca392025-08-20T02:06:47ZengWileyBiochemistry Research International2090-22472090-22552013-01-01201310.1155/2013/914540914540Penetration of Milk-Derived Antimicrobial Peptides into Phospholipid Monolayers as Model BiomembranesWanda Barzyk0Ewa Rogalska1Katarzyna Więcław-Czapla2Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek Street 8, 30-239 Cracow, PolandUMR 7565 CNRS SRSMC, Université de Lorraine, Faculté des Sciences et Technologies, BP 239, 54506 Vandoeuvre-lès-Nancy Cedex, FranceDepartment of Physical Chemistry and Electrochemistry, Faculty of Chemistry, Jagiellonian University, Ingardena 3, 30-060 Cracow, PolandThree antimicrobial peptides derived from bovine milk proteins were examined with regard to penetration into insoluble monolayers formed with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) or 1,2-dipalmitoyl-sn-glycero-3-phospho-rac-(1-glycerol) sodium salt (DPPG). Effects on surface pressure (Π) and electric surface potential (ΔV) were measured, Π with a platinum Wilhelmy plate and ΔV with a vibrating plate. The penetration measurements were performed under stationary diffusion conditions and upon the compression of the monolayers. The two type measurements showed greatly different effects of the peptide-lipid interactions. Results of the stationary penetration show that the peptide interactions with DPPC monolayer are weak, repulsive, and nonspecific while the interactions with DPPG monolayer are significant, attractive, and specific. These results are in accord with the fact that antimicrobial peptides disrupt bacteria membranes (negative) while no significant effect on the host membranes (neutral) is observed. No such discrimination was revealed from the compression isotherms. The latter indicate that squeezing the penetrant out of the monolayer upon compression does not allow for establishing the penetration equilibrium, so the monolayer remains supersaturated with the penetrant and shows an under-equilibrium orientation within the entire compression range, practically.http://dx.doi.org/10.1155/2013/914540
spellingShingle Wanda Barzyk
Ewa Rogalska
Katarzyna Więcław-Czapla
Penetration of Milk-Derived Antimicrobial Peptides into Phospholipid Monolayers as Model Biomembranes
Biochemistry Research International
title Penetration of Milk-Derived Antimicrobial Peptides into Phospholipid Monolayers as Model Biomembranes
title_full Penetration of Milk-Derived Antimicrobial Peptides into Phospholipid Monolayers as Model Biomembranes
title_fullStr Penetration of Milk-Derived Antimicrobial Peptides into Phospholipid Monolayers as Model Biomembranes
title_full_unstemmed Penetration of Milk-Derived Antimicrobial Peptides into Phospholipid Monolayers as Model Biomembranes
title_short Penetration of Milk-Derived Antimicrobial Peptides into Phospholipid Monolayers as Model Biomembranes
title_sort penetration of milk derived antimicrobial peptides into phospholipid monolayers as model biomembranes
url http://dx.doi.org/10.1155/2013/914540
work_keys_str_mv AT wandabarzyk penetrationofmilkderivedantimicrobialpeptidesintophospholipidmonolayersasmodelbiomembranes
AT ewarogalska penetrationofmilkderivedantimicrobialpeptidesintophospholipidmonolayersasmodelbiomembranes
AT katarzynawiecławczapla penetrationofmilkderivedantimicrobialpeptidesintophospholipidmonolayersasmodelbiomembranes