http://www.cnr.it/ontology/cnr/individuo/prodotto/ID13359
The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with DPPC model membranes: a DSC study (Articolo in rivista)
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- The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with DPPC model membranes: a DSC study (Articolo in rivista) (literal)
- Anno
- 2002-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/S0040-6031(02)00074-6 (literal)
- Alternative label
Grasso D., Milardi D., La Rosa C., Impellizzeri G, Pappalardo G.. (2002)
The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with DPPC model membranes: a DSC study
in Thermochimica Acta
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- Grasso D., Milardi D., La Rosa C., Impellizzeri G, Pappalardo G.. (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Grasso D., La Rosa C., Impellizzeri G., Dipartimento di Scienze Chimiche, Università di Catania, Italy.
Milardi D., Pappalardo G., ???? ?Istituto per lo studio delle sostanze naturali di interesse alimentare e chmico farmaceutico, Catania, CNR.
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Milardi D., Pappalardo G. (literal)
- Titolo
- The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with DPPC model membranes: a DSC study (literal)
- Abstract
- Depending on their hydrophobicity, peptides can interact differently with
lipid membranes inducing dramatic modifications into their host systems.
In the present paper, the interaction of a synthetic peptide with a
scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-
His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with 1,2-dipalmitoyl-sn-glycero-
3phosphocholine (DPPC) model membranes has been investigated by
differential scanning calorimetry (DSC), adopting three different
experimental approaches. In the first, the peptide is forced to be
included into the hydrocarbon region of the lipid bilayer, by codissolving
it with the lipid giving rise to mixed multilamellar vesicles-peptide
systems; in the second, this system is passed through an extruder, thus
producing large unilamellar vesicles-peptide systems; in the third, it is
allowed to interact with the external surface of the membrane.
The whole of the DSC results obtained have shown that the incorporation of
the peptide into the lipid bilayer by means of the first method induces a
decrease in the enthalpy of the gel-liquid crystal transition of the
membrane and a shift of the transition to the lower temperatures, thus
resembling, in spite of its prevalently hydrophilic nature, the behavior
of transbilayer hydrophobic peptides. The extrusion of these systems
creates unilamellar vesicles free of peptides but of smaller size as
evidenced by the decreased cooperativity of the transition. The peptide,
added externally to the DPPC model membrane, has no effect on the phase
behavior of the bilayer.
These findings suggest that the effect of the interaction of scrambled
hydrophobic/hydrophilic peptides into lipid bilayers strongly affects the
thermotropic behavior of the host membrane depending on the preparation
method of the lipid/peptide systems. The whole of the results obtained in
the present paper can be useful in approaching studies of bioactive
peptides/lipids systems. © 2002 Elsevier Science B.V. All rights reserved. (literal)
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