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Metal‐triggered hydrogelation of self‐assembling β‐hairpin peptides for bioremediation
Author(s) -
Knerr Patrick James,
Nagarkar Radhika P.,
Schneider Joel P.
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.1010.1
Subject(s) - peptide , chemistry , metal ions in aqueous solution , aqueous solution , amphiphile , metal , circular dichroism , combinatorial chemistry , biophysics , biochemistry , organic chemistry , polymer , copolymer , biology
Peptides have been designed which undergo intermolecular self‐assembly to form rigid, fibrillar hydrogel networks. These peptides are unstructured and soluble in aqueous solution, but can be triggered to fold into an amphiphilic β‐hairpin conformation under specific environmental conditions. Once folded, these hairpins self‐assemble to form the hydrogel. Introduction of metal‐binding functionality into such a system allows for the development of materials in which hydrogelation can be controlled with particular metal ions. This work reports a β‐hairpin peptide incorporating two strategically‐placed cysteine residues, known to bind a host of metal ions including arsenic and zinc. Equimolar addition of methylarsonous acid to an aqueous peptide solution triggers folding and self‐assembly at low peptide concentration (1.0 wt %). Metal‐dependent behavior has been demonstrated using circular dichroism, FTIR, TEM and oscillatory shear rheology. It is envisioned that this system could be responsive to other cysteine‐binding toxic metals, such as mercury and lead. Since the peptide sequence includes only natural L‐amino acids, this peptide can potentially be synthesized biologically and used for large‐scale bioremediation of polluted environments. Funding has been supplied by the Beckman Foundation, the HHMI Undergraduate Biological Sciences Education Program and the NIH.