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Download fileGuided Assembly and Patterning of Intrinsically Fluorescent Amyloid Fibers with Long-Range Order
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posted on 15.01.2021, 16:40 authored by Lisa Hecker, Wenyu Wang, Ioanna Mela, Saeed Fathi, Chetan Poudel, Giancarlo Soavi, Yan Yan Shery Huang, Clemens F. KaminskiFibrillar amyloids exhibit a fascinating
range of mechanical, optical,
and electronic properties originating from their characteristic β-sheet-rich
structure. Harnessing these functionalities in practical applications
has so far been hampered by a limited ability to control the amyloid
self-assembly process at the macroscopic scale. Here, we use core–shell
electrospinning with microconfinement to assemble amyloid-hybrid fibers,
consisting of densely aggregated fibrillar amyloids stabilized by
a polymer shell. Up to centimeter-long hybrid fibers with micrometer
diameter can be arranged into aligned and ordered arrays and deposited
onto substrates or produced as free-standing networks. Properties
that are characteristic of amyloids, including their high elastic
moduli and intrinsic fluorescence signature, are retained in the hybrid
fiber cores, and we show that they fully persist through the macroscopic
fiber patterns. Our findings suggest that microlevel confinement is
key for the guided assembly of amyloids from monomeric proteins.
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macroscopic scalepolymer shellmacroscopic fiber patternsfiber coresmicrolevel confinementβ- sheet-rich structureGuided Assemblyaggregated fibrillar amyloidsamyloid self-assembly processmonomeric proteinsamyloid-hybrid fibersLong-Range Order Fibrillar amyloids...micrometer diameterfluorescence signatureAmyloid Fibers