Surface shear viscosity as a macroscopic probe of amyloid fibril formation at a fluid interface

Soft Matter ◽  
2017 ◽  
Vol 13 (9) ◽  
pp. 1780-1787 ◽  
Author(s):  
Vignesh S. Balaraj ◽  
Philip C. H. Zeng ◽  
Sean P. Sanford ◽  
Samantha A. McBride ◽  
Aditya Raghunandan ◽  
...  
Keyword(s):  
Shear Viscosity ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Fluid Interface ◽  
Surface Shear ◽  
Amyloid Fibril Formation ◽  
Surface Shear Viscosity

scholarly journals Simulated microgravity in the ring-sheared drop

2020 ◽  
Vol 6 (1) ◽  
Author(s):  
Patrick M. McMackin ◽  
Shannon R. Griffin ◽  
Frank P. Riley ◽  
Shreyash Gulati ◽  
Nicholas E. Debono ◽  
...  
Keyword(s):  
Shear Viscosity ◽  
Simulated Microgravity ◽  
Amyloid Fibril ◽  
Space Station ◽  
Fluid Interfaces ◽  
Inertial Forces ◽  
Surface Shear ◽  
Amyloid Fibril Formation ◽  
Shearing Motion ◽  
Surface Shear Viscosity

AbstractThe ring-sheared drop is a module for the International Space Station to study sheared fluid interfaces and their influence on amyloid fibril formation. A 2.54-cm diameter drop is constrained by a stationary sharp-edged ring at some latitude and sheared by the rotation of another ring in the other hemisphere. Shearing motion is conveyed primarily by the action of surface shear viscosity. Here, we simulate microgravity in the laboratory using a density-matched liquid surrounding the drop. Upon shearing, the drop’s deformation away from spherical is found to be a result of viscous and inertial forces balanced against the capillary force. We also present evidence that the deformation increases with increasing surface shear viscosity.

Immunocytochemical Localization of Amyloid Protein AA in the “Dense Fibrillar Inclusions” of the Reticuloendothelical Cells

1977 ◽  
Vol 35 ◽  
pp. 438-439
Author(s):  
T. Shirahama ◽  
M. Skinner ◽  
A.S. Cohen
Keyword(s):  
Amyloid Fibril ◽  
Close Association ◽  
Gel Filtration ◽  
Fibril Formation ◽  
Amyloid Protein ◽  
Electron Microscopic ◽  
Amyloid Deposits ◽  
Amyloid Fibril Formation ◽  
Electron Microscopic Technique ◽  
Lysosomal System

A1thought the mechanisms of amyloidogenesis have not been entirely clarified, proteolysis of the parent proteins may be one of the important steps in the amyloid fibril formation. Recently, we reported that "dense fibrillar inclusions" (DFI), which had the characteristics of lysosomes and contained organized fibrillar profiles as well, were observed in the reticuloendothelial cells in close association with the foci of new amyloid deposits. We considered the findings as evidence for the involvement of lysosomal system in amyloid fibril formation (l). In the present study, we attempted to determine the identity of the contents of the DFI by the use of antisera against the amyloid protein (AA) and an immuno-electron microscopic technique.Amyloidosis was induced in CBA/J mice by daily injections of casein (l). AA was isolated from amyloid-laden spleens by gel filtration and antibody to it was produced in rabbits (2). For immunocytochemistry, the unlabeled antibody enzyme method (3) was employed.

Monitoring the prevention of amyloid fibril formation by α-crystallin

FEBS Journal ◽  
2007 ◽  
Vol 274 (24) ◽  
pp. 6290-6304 ◽  
Author(s):  
Agata Rekas ◽  
Lucy Jankova ◽  
David C. Thorn ◽  
Roberto Cappai ◽  
John A. Carver
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

scholarly journals Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners

2021 ◽  
Vol 296 ◽  
pp. 100510
Author(s):  
Keiichi Yamaguchi ◽  
Masatomo So ◽  
César Aguirre ◽  
Kensuke Ikenaka ◽  
Hideki Mochizuki ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

scholarly journals Investigation of a Peptide Responsible for Amyloid Fibril Formation of β2-Microglobulin byAchromobacterProtease I

2001 ◽  
Vol 277 (2) ◽  
pp. 1310-1315 ◽  
Author(s):  
Gennady V. Kozhukh ◽  
Yoshihisa Hagihara ◽  
Toru Kawakami ◽  
Kazuhiro Hasegawa ◽  
Hironobu Naiki ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Β2 Microglobulin ◽  
Amyloid Fibril Formation

scholarly journals 2P071 Direct observation of burst of amyloid fibril formation by calorimetry(01C. Protein: Property)

2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S170
Author(s):  
Tatsuya Ikenoue ◽  
Young-Ho Lee ◽  
Jozef Kardos ◽  
Yuji Goto
Keyword(s):  
Direct Observation ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Protein Property
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