Morphology transformation via pH-triggered self-assembly of peptides

Langmuir. 2012 Jan 31;28(4):2083-90. doi: 10.1021/la203518w. Epub 2011 Dec 13.

Abstract

Three flexible peptides (P1: (C(17)H(35)CO-NH-GRGDG)(2)KG; P2: (Fmoc-GRGDG)(2)KG; P3: (CH(3)CO-NH-GRGDG)(2)KG) self-assembled to form a variety of morphologically distinct assemblies at different pHs. P1 formed nanofibers at pH 3, then self-assembled into nanospheres with pH up to 6 and further changed to lamellar structures when the pH value was further increased to 10. P2 aggregated into an entwined network structure at pH 3, and then self-assembled into well-defined nanospheres, lamellar structures, and vesicles via adjusting the pH value. However, P3 did not self-assemble into well-ordered nanostructures, presumably due to the absence of a large hydrophobic group. The varying self-assembly behaviors of the peptides at different pHs are attributed to molecular conformational changes. These self-assembled supramolecular materials might contribute to the development of new peptide-based biomaterials.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Hydrogen-Ion Concentration
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular
  • Molecular Conformation
  • Oligopeptides / chemistry*

Substances

  • Oligopeptides
  • arginyl-glycyl-aspartic acid