Effect of disulfide bond formation on β-hairpin hydrogel bulk properties

ORGN 456

Laural Fisher, lfisher@udel.edu1, Juliana K Kretsinger, julianak@chem.udel.edu2, Darrin J. Pochan, pochan@udel.edu3, and Joel P. Schneider, schneijp@udel.edu2. (1) Dept. of Chemistry and Biochemistry, U. of Delaware, 115 Brown Lab, Newark, DE 19716, (2) Department of Chemistry and Biochemistry, University of Delaware, 115 Brown Lab, Newark, DE 19716, (3) Department of Materials Science and Engineering, University of Delaware, 201 DuPont Hall, Newark, DE 19716
MAX 1 is a 20 amino acid, β-hairpin peptide composed of two strands of alternating valine and lysine residues joined by a type II' turn. MAX 1 undergoes self-assembly into rigid, microporous hydrogel material only when correctly folded into a β-hairpin. Since MAX 1 folding from random coil to β-hairpin can be environmentally triggered, material formation can occur with temporal resolution. Hairpin folding and consequent gelation can be initiated by changes in solution pH, ionic strength, or temperature. Three cysteine-containing derivatives of Max 1 are studied to asses the effect of disulfide bond formation on the folding, self-assembly and bulk properties of resulting hydrogels.
 

Bioorganic, Metal-Mediated Reactions, and Molecular Recognition
8:00 PM-10:00 PM, Tuesday, 30 August 2005 Washington DC Convention Center -- Hall A, Poster

Division of Organic Chemistry

The 230th ACS National Meeting, in Washington, DC, Aug 28-Sept 1, 2005