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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| Format: | Article |
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Wiley
2013-01-01
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| 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 |
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| 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. |
| format | Article |
| id | doaj-art-70bc0e919835464ea0f3ac96e07eca39 |
| institution | OA Journals |
| issn | 2090-2247 2090-2255 |
| language | English |
| publishDate | 2013-01-01 |
| publisher | Wiley |
| record_format | Article |
| 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 |