TY - JOUR
T1 - Environmental Control of Amyloid Polymorphism by Modulation of Hydrodynamic Stress
AU - Zhou, Jiangtao
AU - Venturelli, Leonardo
AU - Keiser, Ludovic
AU - Sekatskii, Sergey K.
AU - Gallaire, François
AU - Kasas, Sandor
AU - Longo, Giovanni
AU - Knowles, Tuomas P.J.
AU - Ruggeri, Francesco S.
AU - Dietler, Giovanni
PY - 2021/1
Y1 - 2021/1
N2 - The phenomenon of amyloid polymorphism is a key feature of protein aggregation. Unravelling this phenomenon is of great significance for understanding the underlying molecular mechanisms associated with neurodegenerative diseases and for the development of amyloid-based functional biomaterials. However, the understanding of the molecular origins and the physicochemical factors modulating amyloid polymorphs remains challenging. Herein, we demonstrate an association between amyloid polymorphism and environmental stress in solution, induced by an air/water interface in motion. Our results reveal that low-stress environments produce heterogeneous amyloid polymorphs, including twisted, helical, and rod-like fibrils, whereas high-stress conditions generate only homogeneous rod-like fibrils. Moreover, high environmental stress converts twisted fibrils into rod-like fibrils both in-pathway and after the completion of mature amyloid formation. These results enrich our understanding of the environmental origin of polymorphism of pathological amyloids and shed light on the potential of environmentally controlled fabrication of homogeneous amyloid biomaterials for biotechnological applications.
AB - The phenomenon of amyloid polymorphism is a key feature of protein aggregation. Unravelling this phenomenon is of great significance for understanding the underlying molecular mechanisms associated with neurodegenerative diseases and for the development of amyloid-based functional biomaterials. However, the understanding of the molecular origins and the physicochemical factors modulating amyloid polymorphs remains challenging. Herein, we demonstrate an association between amyloid polymorphism and environmental stress in solution, induced by an air/water interface in motion. Our results reveal that low-stress environments produce heterogeneous amyloid polymorphs, including twisted, helical, and rod-like fibrils, whereas high-stress conditions generate only homogeneous rod-like fibrils. Moreover, high environmental stress converts twisted fibrils into rod-like fibrils both in-pathway and after the completion of mature amyloid formation. These results enrich our understanding of the environmental origin of polymorphism of pathological amyloids and shed light on the potential of environmentally controlled fabrication of homogeneous amyloid biomaterials for biotechnological applications.
KW - air-water interface
KW - amyloid polymorphism
KW - environmental control
KW - hydrodynamic flow
KW - protein aggregation
U2 - 10.1021/acsnano.0c07570
DO - 10.1021/acsnano.0c07570
M3 - Article
AN - SCOPUS:85099011765
SN - 1936-0851
VL - 15
SP - 944
EP - 953
JO - ACS Nano
JF - ACS Nano
IS - 1
ER -