Biophysical Society Thematic Meeting - October 25-30, 2015

Polymers and Self Assembly: From Biology to Nanomaterials

Tuesday Speaker Abstracts

Hydration and Cavities in Amyloid Fibrils and Oligomers Modulated by Hydrostatic Pressure Jerson Silva Federal University of Rio de Janeiro, Brazil No Abstract

Structure-Based Design of Amyloids with Novel Functions for Nanomaterials Cong Liu 1 , Dan Li 1 , Bin Dai 1 , Xiang Zhang 1 , Michael Sawaya 2 , David Eisenberg 2 . 1 Chinese Academy of Sciences, Shanghai, China, 2 UCLA, Los Angeles, CA, USA. Protein can self-assemble into amyloid aggregates with highly ordered hierarchical structure. Amyloid was firstly identified as pathological entities in a variety of devastating human diseases including Parkinson's, Alzheimer's, and Huntington's diseases1. Recently, more and more proteins are found to self-assemble into amyloid with diverse physiological functions, including signal transduction, hormone storage, RNA granules formation, and cell surface adhesion2. Given the favorable properties including high thermal stability, stiffness and biocompatibility, amyloid is acquiring utility as a new class of bionanomaterials. In this work, we developed a general method for the design of functional amyloids with distinct functions, based on the atomic structures of amyloids. We further illustrate the method with two applications3-5. In the first one, we designed amyloid fibrils with lysine condensed and exposed on the fibril surface. We show that designed fibril is capable of capturing carbon dioxide from flue gas. In the second one, we used a newly identified amyloid architecture -- amyloid-like nanosheet as a platform to design a series of effective enhancers for retrovirus transduction. The work demonstrates the potency of the structure-based design method for development of amyloid-based nanomaterials with novel functions. 1. Eisenberg D, Jucker M (2012) The amyloid state of proteins in human diseases. Cell 148(6):1188–1203.2. Maji SK, et al. (2009) Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938):328–332.3. Li D, et al. Structure-based design of functional amyloid materials. J. Am. Chem. Soc, 2014 Dec 31;136(52):18044-51.4. Li D, et al. Designed amyloid fibers as materials for selective carbon dioxide capture. PNAS, 2014, 111, 191-1965. Dai B, et al. Tunable assembly of amyloid- forming peptides into nanosheets as a retrovirus carrier. PNAS, 2015 doi:10.1073/pnas.1416690112.

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