(568f) Templating Mechanism for Self-Assembly of Large Peptide Structures

Large peptide fibers can be spontaneously assembled from combinations of short, hydrophobic peptides (the “template”) and longer, alpha-helix containing peptides (the “adder”).  Nanometer-sized cross-beta “elementary units” form early and can continue to grow into micron-sized fibers at the correct ratio of template to adder.  The self-assembled fibers resemble silk and keratin in size, morphology, and properties but do not require extrusion or spinning to form.  A thermodynamic model is presented to highlight the peptide properties necessary for assembly over 3 orders of magnitude of scale.  Finally, analogies are drawn between in vitro systems and fibrous structures found in bacteria and mussels that show nature may utilize the templating mechanism to form high performance materials for improved modulus, strength, or catalytic rate.