Fast dynamics of semiflexible chain networks of self-assembled peptides.

ABSTRACT: We present the first neutron spin echo (NSE) measurements of self-assembling peptide hydrogel networks to study the fibril dynamics on the nanometer and nanosecond length and time scales. MAX1 and MAX8 are synthetic beta-hairpin peptides that undergo triggered self-assembly at the nanoscale to form a physically cross-linked network of fibrils with a defined cross-section. When subjected to physiological pH and ionic strength (pH 7.4, 150 mM NaCl), the soluble peptides fold into a beta-hairpin and, subsequently, self-assemble to form a structurally rigid hydrogel stabilized by noncovalent cross-links. The sequence of MAX8 is identical to MAX1 with the exception of one single amino acid substitution that reduces the net charge on the peptide. As a result, faster folding and self-assembly kin

SUBMITTER: Branco MC 

PROVIDER: S-EPMC2738993 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature