Forman, CJ and Nickson, AA and Anthony-Cahill, SJ and Baldwin, AJ and Kaggwa, G and Feber, U and Sheikh, K and Jarvis, SP and Barker, PD (2012) The morphology of decorated amyloid fibers is controlled by the conformation and position of the displayed protein. ACS Nano, 6. pp. 1332-1346.Full text not available from this repository.
Self-assembled structures capable of mediating electron transfer are an attractive scientific and technological goal. Therefore, systematic variants of SH3-Cytochrome b(562) fusion proteins were designed to make amyloid fibers displaying heme-b(562) electron transfer complexes. TEM and AFM data show that fiber morphology responds systematically to placement of b(562) within the fusion proteins. UV-vis spectroscopy shows that, for the fusion proteins under test, only half the fiber-borne b(562) binds heme with high affinity. Cofactor binding also improves the AFM imaging properties and changes the fiber morphology through changes in cytochrome conformation. Systematic observations and measurements of fiber geometry suggest that longitudinal registry of subfilaments within the fiber, mediated by the interaction and conformation of the displayed proteins and their interaction with surfaces, gives rise to the observed morphologies, including defects and kinks. Of most interest is the role of small molecule modulation of fiber structure and mechanical stability. A minimum complexity model is proposed to capture and explain the fiber morphology in the light of these results. Understanding the complex interplay between these factors will enable a fiber design that supports longitudinal electron transfer.
|Uncontrolled Keywords:||Amyloid Cytochrome b Group Electron Transport Heme Microscopy, Atomic Force Models, Molecular Protein Multimerization Recombinant Fusion Proteins src Homology Domains|
|Divisions:||Div E > Production Processes|
|Depositing User:||Unnamed user with email email@example.com|
|Date Deposited:||16 Jul 2015 13:16|
|Last Modified:||05 Sep 2015 00:57|