Modular genetic design of multi-domain functional amyloids: insights into self-assembly and functional properties.

ABSTRACT: Engineering functional amyloids through a modular genetic strategy represents new opportunities for creating multifunctional molecular materials with tailored structures and performance. Despite important advances, how fusion modules affect the self-assembly and functional properties of amyloids remains elusive. Here, using Escherichia coli curli as a model system, we systematically studied the effect of flanking domains on the structures, assembly kinetics and functions of amyloids. The designed amyloids were composed of E. coli biofilm protein CsgA (as amyloidogenic cores) and one or two flanking domains, consisting of chitin-binding domains (CBDs) from Bacillus circulans chitinase, and/or mussel foot proteins (Mfps). Incorporation of fusion domains did not disrupt t

SUBMITTER: Cui M 

PROVIDER: S-EPMC6461117 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature