Hydrophobic surfaces help reduce harmful protein fibril formation

Scilight ◽  
2020 ◽  
Vol 2020 (36) ◽  
pp. 361110
Author(s):  
Savannah Mandel
2019 ◽  
Vol 32 (2) ◽  
pp. 77-85
Author(s):  
Mohammad Ashhar I Khan ◽  
Ulrich Weininger ◽  
Sven Kjellström ◽  
Shashank Deep ◽  
Mikael Akke

Abstract Intracellular aggregates of superoxide dismutase 1 (SOD1) are associated with amyotrophic lateral sclerosis. In vivo, aggregation occurs in a complex and dense molecular environment with chemically heterogeneous surfaces. To investigate how SOD1 fibril formation is affected by surfaces, we used an in vitro model system enabling us to vary the molecular features of both SOD1 and the surfaces, as well as the surface area. We compared fibril formation in hydrophilic and hydrophobic sample wells, as a function of denaturant concentration and extraneous hydrophobic surface area. In the presence of hydrophobic surfaces, SOD1 unfolding promotes fibril nucleation. By contrast, in the presence of hydrophilic surfaces, increasing denaturant concentration retards the onset of fibril formation. We conclude that the mechanism of fibril formation depends on the surrounding surfaces and that the nucleating species might correspond to different conformational states of SOD1 depending on the nature of these surfaces.


2001 ◽  
Vol 72 (4) ◽  
pp. 1681-1687 ◽  
Author(s):  
Gerardo M. Castillo ◽  
Widia Lukito ◽  
Thomas N. Wight ◽  
Alan D. Snow

Life Sciences ◽  
2002 ◽  
Vol 70 (13) ◽  
pp. 1555-1564 ◽  
Author(s):  
Yoichi Kiuchi ◽  
Yoshihiko Isobe ◽  
Kiyomi Fukushima

Author(s):  
E. Kiran Kumar ◽  
Neshatul Haque ◽  
N. Prakash Prabhu

2001 ◽  
Vol 305 (2) ◽  
pp. 119-122 ◽  
Author(s):  
Yoichi Kiuchi ◽  
Yoshihiko Isobe ◽  
Kiyomi Fukushima

2019 ◽  
Vol 116 (3) ◽  
pp. 195a-196a
Author(s):  
Carlos M. Perez ◽  
Ghanim Ullah ◽  
Tatiana Miti ◽  
Martin Muschol

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