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Driving Forces for Adsorption of Amphiphilic Peptides to the Air-Water Interface
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2010 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 114, no 34, 11093-11101 p.Article in journal (Refereed) Published
Abstract [en]

We have studied the partitioning of amphiphilic peptides at the air-water interface. The free energy of adsorption from bulk to interface was calculated by determining the potential of mean force via atomistic molecular dynamics simulations. To this end a method is introduced to restrain or constrain the center of mass of a group of molecules in a periodic system. The model amphiphilic peptides are composed of alternating valine and asparagine residues. The decomposition of the free energy difference between the bulk and interface is studied for different peptide block lengths. Our analysis revealed that for short amphiphilic peptides the surface driving force dominantly stems from the dehydration of hydrophobic side chains. The only opposing force is associated with the loss of orientational freedom of the peptide at the interface. For the peptides studied, the free energy difference scales linearly with the size of the molecule, since the peptides mainly adopt extended conformations both in bulk and at the interface. The free energy difference depends strongly on the water model, which can be rationalized through the hydration thermodynamics of hydrophobic solutes. Finally, we measured the reduction of the surface tension associated with complete coverage of the interface with peptides.

Place, publisher, year, edition, pages
2010. Vol. 114, no 34, 11093-11101 p.
National Category
Natural Sciences
URN: urn:nbn:se:su:diva-50189DOI: 10.1021/jp1024922ISI: 000281128700020OAI: diva2:381862
authorCount :4Available from: 2010-12-29 Created: 2010-12-21 Last updated: 2010-12-29Bibliographically approved

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Hess, Berk
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