Cationic gemini surfactant (16-4-16) interact electrostatically with anionic plant lectin and facilitates amyloid fibril formation at neutral pH

2017 ◽  
Vol 522 ◽  
pp. 494-502 ◽  
Author(s):  
Javed Masood Khan ◽  
Mohd. Shahnawaz Khan ◽  
Atiyatul Qadeer ◽  
Mohammad A. Alsenaidy ◽  
Anwar Ahmed ◽  
...  
Keyword(s):  
Gemini Surfactant ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Plant Lectin ◽  
Cationic Gemini Surfactant ◽  
Neutral Ph ◽  
Amyloid Fibril Formation

scholarly journals Cationic gemini surfactant stimulates amyloid fibril formation in bovine liver catalase at physiological pH. A biophysical study

RSC Advances ◽  
2020 ◽  
Vol 10 (71) ◽  
pp. 43751-43761
Author(s):  
Javed Masood Khan ◽  
Ajamaluddin Malik ◽  
Md. Tabish Rehman ◽  
Mohamed F. AlAjmi ◽  
Mohammad Z. Ahmed ◽  
...  
Keyword(s):  
Gemini Surfactant ◽  
Amyloid Fibril ◽  
Bovine Liver ◽  
Fibril Formation ◽  
Conformational Switching ◽  
Cationic Gemini Surfactant ◽  
Amyloid Fibril Formation ◽  
Biophysical Study ◽  
Bovine Liver Catalase ◽  
Amyloid Fibrillation

Surfactant molecules stimulate amyloid fibrillation and conformational switching in proteins but the mechanisms by which they accomplish these effects are unclear.

scholarly journals A cell-based high-throughput screening method to directly examine transthyretin amyloid fibril formation at neutral pH

2019 ◽  
Vol 294 (29) ◽  
pp. 11259-11275 ◽  
Author(s):  
Mitsuharu Ueda ◽  
Masamitsu Okada ◽  
Mineyuki Mizuguchi ◽  
Barbara Kluve-Beckerman ◽  
Kyosuke Kanenawa ◽  
...  
Keyword(s):  
High Throughput ◽  
High Throughput Screening ◽  
Amyloid Fibril ◽  
Screening Method ◽  
Fibril Formation ◽  
Neutral Ph ◽  
Amyloid Fibril Formation ◽  
A Cell

scholarly journals 3P045 Direct observation ofβ_2-microglobulin amyloid fibril formation at neutral pH

2005 ◽  
Vol 45 (supplement) ◽  
pp. S215
Author(s):  
D. Ozawa ◽  
T. Ban ◽  
A. Kameda ◽  
H. Naiki ◽  
Y. Goto
Keyword(s):  
Direct Observation ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Neutral Ph ◽  
Amyloid Fibril Formation

scholarly journals Heating during agitation of β2-microglobulin reveals that supersaturation breakdown is required for amyloid fibril formation at neutral pH

2019 ◽  
Vol 294 (43) ◽  
pp. 15826-15835 ◽  
Author(s):  
Masahiro Noji ◽  
Kenji Sasahara ◽  
Keiichi Yamaguchi ◽  
Masatomo So ◽  
Kazumasa Sakurai ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Β2 Microglobulin ◽  
Neutral Ph ◽  
Amyloid Fibril Formation

Amyloid fibril formation by pepsin in neutral pH at room temperature

Soft Matter ◽  
2013 ◽  
Vol 9 (48) ◽  
pp. 11457 ◽  
Author(s):  
Subhajit Ghosh ◽  
Subhrajyoti Dolai ◽  
Joykrishna Dey
Keyword(s):  
Room Temperature ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Neutral Ph ◽  
Amyloid Fibril Formation

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.

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