Heavy metal ion hydrogelation of a self-assembling peptide via cysteinyl chelation

Hydrogel materials are finding use in heavy metal ion detection and remediation. MBHP is a twenty-residue peptide capable of undergoing hydrogelation in response to heavy metal ion binding. The unstructured peptide binds monomethylarsonous acid, Pb2+, Zn2+, Cd2+ or Hg2+ and subsequently folds into an amphiphilic beta-hairpin that rapidly self-assembles into a beta-sheet rich fibrillar network as shown by CD spectroscopy and transmission electron microscopy. LCMS shows that MBHP binds metal ions with a 1 : 1 stoichiometry. Oscillatory rheology indicates that moderately rigid hydrogels are formed as a result of metal ion binding, peptide folding and ultimate self-assembly with storage moduli (G') ranging from similar to 1000-4000 Pa.