The position of hydrophobic residues tunes peptide self-assembly

Christian Bortolini, Lei Liu, Thomas M. A. Gronewold, Chen Wang, Flemming Besenbacher, MD Dong

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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.
Original languageEnglish
JournalSoft Matter
Volume10
Issue31
Pages (from-to)5656-5661
Number of pages6
ISSN1744-683X
DOIs
Publication statusPublished - 2014

Keywords

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

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