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Polymers and Self Assembly: From Biology to Nanomaterials
Wednesday Speaker Abstracts
Self-Assembling Peptide Based Materials for Regenerative Medicine
Aline Miller
.
University of Manchester, Manchester, United Kingdom.
The development of highly functional, tailored soft materials is arguably one of the most
important challenges of material science for the next decade. Self-assembling peptides have been
highlighted as one of the most promising building blocks for future material design where
individual molecules are held together via strong, yet irreversible bonds, imparting strength to
the material. The translation of these soft materials into commercial applications is starting to
become a reality with the advent of routine procedures for peptide synthesis and purification in
both the lab and industrial scale, thus making them easily accessible at a reasonable cost.
Consequently design rules for the self-assembly route of the different peptide systems and final
material structure and properties are emerging, but these typically provide bare materials that
lack the ability to adapt to their environment. Here several different strategies developed in our
group will be outlined for the fabrication of functional, responsive and active materials based on
ionic-complementary self-assembling octa-peptides. Several examples of the different types of
functionalities that can be incorporated will be outlined, thus covering a wide range of
application areas including controlling cell culture, targeted and temporal release of therapeutics,
biosensors and biocatalysis for fine chemical manufacturing.
Protein Self-Assembly by Rational Chemical Design
F. Akif Tezcan
.
University of California, San Diego, La Jolla, USA.
Proteins represent the most versatile building blocks available to living organisms for
constructing functional materials and molecular devices. Underlying this versatility is an
immense structural and chemical heterogeneity that renders the programmable self-assembly of
protein an extremely challenging design task. To circumvent the challenge of designing
extensive non-covalent interfaces for controlling protein self-assembly, we have endeavored to
use rational, chemical bonding strategies based on metal coordination and disulfide bonding.
These approaches have resulted in discrete or infinite, 1-, 2- and 3D protein architectures that
display structural order over large lengths scales, yet are dynamic and stimuli-responsive, and
possess emergent physical and functional properties.