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

  1. Author:
    Knerr, P. J.
    Branco, M. C.
    Nagarkar, R.
    Pochan, D. J.
    Schneider, J. P.

  2. Author Address

    [Branco, Monica C.; Schneider, Joel P.] NCI, Biol Chem Lab, Frederick, MD 21701 USA. [Knerr, Patrick J.; Nagarkar, Radhika] Univ Delaware, Dept Chem & Biochem, Newark, DE 19716 USA. [Pochan, Darrin J.] Univ Delaware, Dept Mat Sci & Engn, Newark, DE 19716 USA.;Schneider, JP (reprint author), NCI, Biol Chem Lab, Frederick, MD 21701 USA;schneiderjp@mail.nih.gov
    1. Year: 2012
    2. Date: Jan 28
  2. Journal: Journal of Materials Chemistry
    1. 22
    2. 4
    3. Pages: 1352-1357
  4. Type of Article: Article
  5. ISSN: 0959-9428
  1. Abstract:

    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, Pb(2+), Zn(2+), Cd(2+) or Hg(2+) 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.

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External Sources

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  2. DOI: 10.1039/c1jm14418a
  3. View record in Web of Science®
  4. WOS: 000298878100016

Library Notes

  1. Fiscal Year: FY2011-2012
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