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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.