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Updated: Apr 27, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
The position of hydrophobic residues tunes peptide self-assembly
Christian Bortolini1, Lei Liu, Thomas M A Gronewold
1Interdisciplinary Nanoscience Center (iNANO), Gustav Wieds 14, Building 1590, Aarhus C., Denmark. dong@inano.au.dk.
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.
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