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Emergence of amyloidic fibrillation in 2D-ordered Langmuir-Blodgett protein multilayers upon heating
- Publication Year :
- 2020
- Publisher :
- American Institute of Physics Inc., 2020.
-
Abstract
- Langmuir–Blodgett protein nanofilms can serve as templates for nucleation and growth of protein crystals. This functionality can be enhanced by thermal annealing. While surface ordering of the multilayered nanofilms and an improvement of the correlation between the layers during thermal annealing have been revealed by atomic force microscopy and grazing-incidence small-angle x-ray scattering, information on the structure developing in the bulk of nanofilms is lacking. In this paper, we report on scanning x-ray nanodiffraction experiments of penicillin-G-acylase multilayers deposited on Si3N4 membranes and annealed at 150 °C. While the annealed multilayer has remained mostly featureless, we observe locally globular aggregates and filamentous spherulites based on nanofibrillar subunits with cross-β amyloidic motifs.
- Subjects :
- 010302 applied physics
Materials science
Physics and Astronomy (miscellaneous)
Atomic force microscopy
Scattering
Nucleation
02 engineering and technology
021001 nanoscience & nanotechnology
01 natural sciences
Langmuir–Blodgett film
Membrane
Chemical engineering
0103 physical sciences
0210 nano-technology
Protein crystallization
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....5951fa891810de405c2369f486a062cb