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Self-Assembly of Protein Fibrils in Microgravity

Dylan Bell
Dylan Bell
, 
Samuel Durrance
Samuel Durrance
, 
Daniel Kirk
Daniel Kirk
, 
Hector Gutierrez
Hector Gutierrez
, 
Daniel Woodard
Daniel Woodard
, 
Jose Avendano
Jose Avendano
, 
Joseph Sargent
Joseph Sargent
, 
Caroline Leite
Caroline Leite
, 
Beatriz Saldana
Beatriz Saldana
, 
Tucker Melles
Tucker Melles
, 
Samantha Jackson
Samantha Jackson
 y 
Shaohua Xu
Shaohua Xu
   | 20 jul 2020
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Article Category: Research Article
Publicado en línea: 20 jul 2020
Páginas: 10 - 26
DOI: https://doi.org/10.2478/gsr-2018-0002
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© 2018 Dylan Bell et al., published by Sciendo
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Figure 1

AFM images of lysozyme aggregation showing advanced stages of the amyloid fibril formation process (Woodard et al., 2014). Left: the merging of fibrils into a helix configuration is indicated by the two arrows. Right: A tangled interlocking network prevents fibrils from rotating and halts helix formation. (Note the different image scales.)
AFM images of lysozyme aggregation showing advanced stages of the amyloid fibril formation process (Woodard et al., 2014). Left: the merging of fibrils into a helix configuration is indicated by the two arrows. Right: A tangled interlocking network prevents fibrils from rotating and halts helix formation. (Note the different image scales.)

Figure 2

Deformation of lysozyme samples under different load forces (force set-points). Each data point is an average of 20 lysozyme fibril height measurements made at each force set-point. Error bars are the measurement standard deviations. The dashed line is a linear fit to the data.
Deformation of lysozyme samples under different load forces (force set-points). Each data point is an average of 20 lysozyme fibril height measurements made at each force set-point. Error bars are the measurement standard deviations. The dashed line is a linear fit to the data.

Figure 3

An exploded view of the SABOL experiment. The hardware was designed to fit within the volume, mass, and power constraints of a 1U NanoLab module. There are 9 independently operated vials used to provide a range of incubation times covering the growth phase of lysozyme fibrils.
An exploded view of the SABOL experiment. The hardware was designed to fit within the volume, mass, and power constraints of a 1U NanoLab module. There are 9 independently operated vials used to provide a range of incubation times covering the growth phase of lysozyme fibrils.

Figure 4

Fully assembled SABOL NanoLab with samples loaded. Unit shown just before the outer shell was installed.
Fully assembled SABOL NanoLab with samples loaded. Unit shown just before the outer shell was installed.

Figure 5

Cross-section of polypropylene vials before and after actuation.
Cross-section of polypropylene vials before and after actuation.

Figure 6

ISS Vial Temperature verses Time. Temperature profiles for each of the ISS NanoLab vials show the time when each heater was turned on, raising the temperature to within the aggregation range (Hill et al., 2009; Woodard et al., 2014), held there for its incubation period, and then turned off.
ISS Vial Temperature verses Time. Temperature profiles for each of the ISS NanoLab vials show the time when each heater was turned on, raising the temperature to within the aggregation range (Hill et al., 2009; Woodard et al., 2014), held there for its incubation period, and then turned off.

Figure 7

Top support plate that holds the vials in place. The stepper motor shafts stick through this support, clearly showing that only vial positions 5, 6, and 8 were actuated.
Top support plate that holds the vials in place. The stepper motor shafts stick through this support, clearly showing that only vial positions 5, 6, and 8 were actuated.

Figure 8

Temperature profile of each vial within the G-C NanoLab. The graph shows the time when each heater was turned on, raising the temperature to within the aggregation range (Hill et al., 2009; Woodard et al., 2014). The bold lines represent the temperature profiles from the vials that incubated for periods of time close to the 3 vials that fully actuated in the ISS NanoLab.
Temperature profile of each vial within the G-C NanoLab. The graph shows the time when each heater was turned on, raising the temperature to within the aggregation range (Hill et al., 2009; Woodard et al., 2014). The bold lines represent the temperature profiles from the vials that incubated for periods of time close to the 3 vials that fully actuated in the ISS NanoLab.

Figure 9

AFM image of solution from ISS vial 8, 7.75 days of incubation, 5 x 5 μm FOV.
AFM image of solution from ISS vial 8, 7.75 days of incubation, 5 x 5 μm FOV.

Figure 10

Lysozyme fibrils formed in microgravity on the ISS versus lysozyme fibrils formed in the G-C unit under the effects of gravity. All images have a 5 μm FOV.
Lysozyme fibrils formed in microgravity on the ISS versus lysozyme fibrils formed in the G-C unit under the effects of gravity. All images have a 5 μm FOV.

Figure 11

Heights of protein fibrils formed in microgravity (ISS) compared to protein fibrils formed in a Ground-Control (G-C) experiment.
Heights of protein fibrils formed in microgravity (ISS) compared to protein fibrils formed in a Ground-Control (G-C) experiment.

NanoLab Timeline (EST).

Plugged InDuration
ISS NanoLabJan. 13th 1:22 PM25d 18h 28m
G-C NanoLabFeb. 10th 4:41 PM25d 18h 28m
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