Biophysical Society Thematic Meeting - October 25-30, 2015

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.

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