Hydrogel Scaffolds of Amphiphilic and Acidic β-Sheet Peptides

Authors


  • This work was supported by B. G. Negev, the Horowitz Foundation, and by the Ministry of Science, Israel.

Abstract

Amphiphilic and acidic β-sheet-forming peptides (AAβPs) having the sequence Pro-Y-(Z-Y)5-Pro, Y = Glu or Asp and Z = Phe or Leu may assemble into hydrogel structures at near neutral pH values, several units higher than the intrinsic pKa of their acidic amino acid side chains. The bottom-to-top design strategy enables the rationally supported association between the peptides' amino acids composition and bulk pH hydrogelation. Hydrogen bonds between the acidic amino acids side chains in the β-sheet structure are found to contribute substantially to the stabilization of AAβPs hydrogels. The negatively charged peptides are also found to form gels at lower concentration in presence of calcium ions. Bone forming cells may be cultured on two-dimensional films of AAβPs hydrogels that form at physiological pH values as well as within three dimensional hydrogel matrices. These acidic-rich peptides hydrogels may become advantageous in applications related to engineering of mineralized tissues providing controllable, multifunctional calcified scaffolds to affect both the biological activity and the inorganic mineralization.

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