Peptide amphiphile nanofibers for biomimetic mineralization

ORGN 48

Virany M. Yuwono, vmyuwono@rice.edu and Jeffrey Hartgerink. Department of Chemistry, Rice University, 6100 Main St., Houston, TX 77005
Biomineralization is a widespread phenomenon in nature that creates well-organized structures, such as bone, teeth and shells. Such a high degree of control over the structure of inorganic material is desired in synthetic systems. Peptide amphiphile (PA) nanofibers are attractive self-assembling systems for biomimetic mineralization. The PA self-assembly behavior is easily controlled by integrating pH-sensitive amino acid residues into the peptide sequence. In this work, PAs serve as directing agents and templates for mineralization. Hollow silica nanotubes with tunable dimensions are synthesized by sol-gel condensation of TEOS on the PA nanofiber template followed by calcination. PA nanofibers direct silica mineralization by providing nucleation sites and catalyze TEOS hydrolysis. The catalytic activities of PAs containing lysine, histidine or glutamic acid were compared and only PAs containing lysine or histidine were found to be good catalytic templates. Depending on the reaction conditions, and the size of the PA assembly, the nanotube wall thickness could be varied between 5-9 nm.
 

Biologically-Related Molecules and Processes
1:00 PM-5:00 PM, Sunday, March 25, 2007 McCormick Place Lakeside -- Room E350, Level 3, Oral

Division of Organic Chemistry

The 233rd ACS National Meeting, Chicago, IL, March 25-29, 2007