Guided Assembly and Patterning of Intrinsically Fluorescent Amyloid Fibers with Long-Range Order
mediaposted on 15.01.2021, 16:40 by Lisa Hecker, Wenyu Wang, Ioanna Mela, Saeed Fathi, Chetan Poudel, Giancarlo Soavi, Yan Yan Shery Huang, Clemens F. Kaminski
Fibrillar 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