Formation of oriented polypeptides on Au(111) surface depends on the secondary structure controlled by peptide length

J Pept Sci. 2006 Jun;12(6):396-402. doi: 10.1002/psc.740.

Abstract

We synthesized three different lengths of poly(L-lysine) containing an -SH group at the terminal (PLL(n)-SH, n (polymerization degree) = 4, 10, 30) and adsorbed them on an Au(111) surface. To analyze the formation process and the structure of self-assembled monolayers (SAMs), we used atomic force microscopy (AFM) and Fourier transform infrared reflection absorption spectra (FT-IR RAS). At the initial stage of SAM growth, formation of nanosize domains was confirmed by AFM imaging. The alpha-helical PLL(30)-SH exhibited a well-defined SAM structure after adsorption reached equilibrium. The alpha-helical PLL(30)-SH was almost perpendicular to the gold surface and exhibited interesting molecular packing due to the secondary structure of PLL(30)-SH and the underlying Au(111) array. The tilt angle of the helix axis from the substrate normal was estimated to be about 50 degrees (AFM) and 44 degrees (FT-IR RAS) respectively. On the other hand, PLL(4)-SH and PLL(10)-SH formed beta-sheet-type SAMs on the Au(111) surface based on the structure determined by FT-IR RAS spectrum.

MeSH terms

  • Adsorption
  • Circular Dichroism
  • Gold / chemistry*
  • Microscopy, Atomic Force
  • Molecular Weight
  • Peptides / chemical synthesis*
  • Peptides / chemistry
  • Polylysine / chemistry*
  • Protein Structure, Secondary
  • Spectroscopy, Fourier Transform Infrared
  • Surface Properties

Substances

  • Peptides
  • Polylysine
  • Gold