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Ordered Langmuir-Blodgett films of amphiphilic β-hairpin peptides imaged by atomic force microscopy

  • Evan T. Powers
  • , Sung Ik Yang
  • , Charles M. Lieber
  • , Jeffery W. Kelly

Research output: Contribution to journalArticlepeer-review

57 Citations (Scopus)

Abstract

Peptide length affects the size of the ridges observed in the atomic force microscopy (AFM) images of the Langmuir-Blodgett films of amphiphilic peptides: Well-ordered from a 14-residue amphiphilic peptide (left), while ordered LB films with a wider lattice (right) are obtained from an 18-residue peptide. The 100 nm x 100 nm images pictured were obtained by AFM using carbon nanotube tips.

Original languageEnglish
Pages (from-to)127-130
Number of pages4
JournalAngewandte Chemie - International Edition
Volume41
Issue number1
DOIs
Publication statusPublished - 4 Jan 2002

Keywords

  • Nanostructures
  • Peptides
  • Scanning probe microscopy
  • Self-assembly
  • Thin films

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