Peptide nanospheres self-assembled from a modified β-annulus peptide of Sesbania mosaic virus

Biopolymers. 2016 Nov 4;106(4):470-5. doi: 10.1002/bip.22774.


A novel β-annulus peptide of Sesbania mosaic virus bearing an FKFE sequence at the C terminus was synthesized, and its self-assembling behavior in water was investigated. Dynamic light scattering and transmission electron microscopy showed that the β-annulus peptide bearing an FKFE sequence self-assembled into approximately 30 nm nanospheres in water at pH 3.8, whereas the β-annulus peptide without the FKFE sequence afforded only irregular aggregates. The peptide nanospheres possessed a definite critical aggregation concentration (CAC = 26 μM), above which the size of nanospheres were nearly unaffected by the peptide concentration. The formation of peptide nanospheres was significantly affected by pH; the peptide did not form any assemblies at pH 2.2, whereas larger aggregates were formed at pH 6.4-11.6. © 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 470-475, 2016.

Keywords: nanosphere; self-assembly; viral capsid; β-annulus peptide.

MeSH terms

  • Mosaic Viruses / chemistry*
  • Nanospheres / chemistry*
  • Peptides* / chemical synthesis
  • Peptides* / chemistry
  • Sesbania / virology*
  • Viral Proteins / chemistry*


  • Peptides
  • Viral Proteins