The position of hydrophobic residues tunes peptide self-assembly

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  • Christian Bortolini, National Center for Nanoscience and Technology (NCNST), Beijing, Denmark
  • Lei Liu, Institute for Advanced Materials, Jiangsu University, Zhenjiang, Denmark
  • Thomas M. A. Gronewold, SAW Instruments GmbH Schwertberger, Germany
  • Chen Wang, National Center for Nanoscience and Technology (NCNST), Beijing, Unknown
  • Flemming Besenbacher
  • MD Dong
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.
Original languageEnglish
JournalSoft Matter
Volume10
Issue31
Pages (from-to)5656-5661
Number of pages6
ISSN1744-683X
DOIs
Publication statusPublished - 2014

    Research areas

  • BETA-AMYLOID FIBRILS, GLUCAGON FIBRILLATION, CYTOTOXICITY, BIOMATERIALS, POLYMORPHISM, FRAGMENTS, PH

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