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Abstract EANA2024-128


Microgravity and DNA presence as factors in aggregation pathway selection toward peptides fibrilization

Anna Adamczyk1, Tomasz Zajkowski 2,3, Marzena Krzek4,5
1AGH University of Kraków, Al. A. Mickiewicza 30, 30-059 Cracov, Poland 2 Blue Marble Space Institute of Science, 1001 4th Ave, Suite 1006, Seattle, WA 98154, United States 3 Polish Astrobiology Society, Pasteura 1, 02-093 Warsaw, Poland 4 ECHIA Lab, Józefa Marcika 27, 30-443 Cracov, Poland 5 The Analog Astronaut Training Center, Koło Strzelnicy 8A, 30-219 Cracov, Poland


Protein aggregation towards fibrils has been extensively studied since this phenomenon contributes to amyloid disease etiology and is used in biomaterials preparation [1], [2]. Mass transfer next to the air-water interface plays a pivotal role during this process. For fibrilization, few reports show the influence of low-complex mass transfer types. While looking at the micro-scale mass transfer, the gravitational level is pivotal since it alters movements of higher and lower density masses around the evolving solute [3] and further probability of their interactions. Until now, very few reports describe the gravity effect on fibril formation [4]–[6] and the studies published start from fully homogenous solutions which includes nucleation phase.

The influence of DNA presence is of great relevance in understanding diseases etiology in which proteins fibrilization is involved including diabetes and neurogenerative diseases e.g. Parkinson’s [7].

Our study addresses the effect of rpm machine-generated microgravity on protein and peptides aggregation pathway selection for homogenous and initially temperature-destabilized solutions in the presence and absence of DNA. The findings have shown that microgravity was more detrimental fibrilization factor for the selection of aggregation after initial destabilization of homogeneous solution. For homogenous solution the dominant factor pathway selection had DNA presence and microgravity modulated the final morphology. Our poster will discuss further details

 

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[3]         K. Jackson et al., “Microgravity Crystal Formation,” Crystals, vol. 14, no. 1, 2024.

[4]         M. Krzek, S. Stroobants, P. Gelin, W. De Malsche, and D. Maes, “Influence of Centrifugation and Shaking on the Self-Assembly of Lysozyme Fibrils,” Biomolecules, vol. 12, no. 12, 2022.

[5]         J. Zhou et al., “Effects of sedimentation, microgravity, hydrodynamic mixing and air-water interface on α-synuclein amyloid formation,” Chem. Sci., vol. 11, no. 14, pp. 3687–3693, 2020.

[6]         D. Bell et al., “Self-Assembly of Protein Fibrils in Microgravity,” Gravitational Sp. Res., vol. 6, no. 1, pp. 10–26, 2018.

[7]       T.J. Litberg, S. Horowitz, ‘’Roles of Nucleic Acids in Protein Folding, Aggregation, and Disease,’’ ACS Chem. Biol. vol. 19, no 4, 809–823, 2024