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Issue 24, 2014
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pH-dependent self-assembly of EAK16 peptides in the presence of a hydrophobic surface: Coarse-grained molecular dynamics simulation

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Abstract

Self-assembly behavior of the three types of ionic peptide, EAK16, is studied in the presence of a hydrophobic surface using coarse-grained molecular dynamics simulations at three pH ranges of the solution. It is found that the peptide chains of all the three types assemble on the hydrophobic surface. EAK16-I and EAK16-II peptides assemble into ribbon-like structures, regardless of the value of pH. EAK16-IV peptide chains, however, assemble into ribbon-like structures at low and high pH ranges and form disc-shaped assemblies on the hydrophobic surface at the isoelectric point, pH = 7. Strong intra-chain electrostatic interactions in the case of EAK16-IV peptide play the main role in dependence of its self-assembly behavior on pH and the different morphology of its assembly relative to those of the two other types. Kinetics of growth of the assemblies on the hydrophobic surface is also studied.

Graphical abstract: pH-dependent self-assembly of EAK16 peptides in the presence of a hydrophobic surface: Coarse-grained molecular dynamics simulation

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Publication details

The article was received on 08 Feb 2014, accepted on 17 Feb 2014 and first published on 17 Feb 2014


Article type: Paper
DOI: 10.1039/C4SM00307A
Citation: Soft Matter, 2014,10, 4248-4257

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    pH-dependent self-assembly of EAK16 peptides in the presence of a hydrophobic surface: Coarse-grained molecular dynamics simulation

    S. Emamyari and H. Fazli, Soft Matter, 2014, 10, 4248
    DOI: 10.1039/C4SM00307A

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