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Issue 31, 2014
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The position of hydrophobic residues tunes peptide self-assembly

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Abstract

The final structure and properties of synthetic peptides mainly depend on their sequence composition and experimental conditions. This work demonstrates that a variation in the positions of hydrophobic residues within a peptide sequence can tune the self-assembly. Techniques employed are atomic force microscopy, transmission electron microscopy and an innovative method based on surface acoustic waves. In addition, a systematic investigation on pH dependence was carried out by utilizing constant experimental parameters.

Graphical abstract: The position of hydrophobic residues tunes peptide self-assembly

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Publication details

The article was received on 15 May 2014, accepted on 20 Jun 2014 and first published on 23 Jun 2014


Article type: Communication
DOI: 10.1039/C4SM01065E
Author version available: Download Author version (PDF)
Citation: Soft Matter, 2014,10, 5656-5661
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    The position of hydrophobic residues tunes peptide self-assembly

    C. Bortolini, L. Liu, T. M. A. Gronewold, C. Wang, F. Besenbacher and M. Dong, Soft Matter, 2014, 10, 5656
    DOI: 10.1039/C4SM01065E

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