Elucidating the Kinetics of β-Amyloid Fibril Formation

2005 ◽  
pp. 106-118 ◽  
Author(s):  
Nadia J. Edwin ◽  
Grigor B. Bantchev ◽  
Paul S. Russo ◽  
Robert P. Hammer ◽  
Robin L. McCarley
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Β Amyloid ◽  
Kinetics Of

scholarly journals The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid

2021 ◽  
Vol 118 (3) ◽  
pp. e2014442118
Author(s):  
Nir Salinas ◽  
Einav Tayeb-Fligelman ◽  
Massimo D. Sammito ◽  
Daniel Bloch ◽  
Raz Jelinek ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Membrane Damage ◽  
Fibril Formation ◽  
Regulation Mechanism ◽  
Bacterial Cells ◽  
Amyloid Fibril Formation ◽  
Β Amyloid ◽  
Β Sheets

Antimicrobial activity is being increasingly linked to amyloid fibril formation, suggesting physiological roles for some human amyloids, which have historically been viewed as strictly pathological agents. This work reports on formation of functional cross-α amyloid fibrils of the amphibian antimicrobial peptide uperin 3.5 at atomic resolution, an architecture initially discovered in the bacterial PSMα3 cytotoxin. The fibrils of uperin 3.5 and PSMα3 comprised antiparallel and parallel helical sheets, respectively, recapitulating properties of β-sheets. Uperin 3.5 demonstrated chameleon properties of a secondary structure switch, forming mostly cross-β fibrils in the absence of lipids. Uperin 3.5 helical fibril formation was largely induced by, and formed on, bacterial cells or membrane mimetics, and led to membrane damage and cell death. These findings suggest a regulation mechanism, which includes storage of inactive peptides as well as environmentally induced activation of uperin 3.5, via chameleon cross-α/β amyloid fibrils.

scholarly journals Effect of Association State and Conformational Stability on the Kinetics of Immunoglobulin Light Chain Amyloid Fibril Formation at Physiological pH

2002 ◽  
Vol 277 (15) ◽  
pp. 12657-12665 ◽  
Author(s):  
Pierre O. Souillac ◽  
Vladimir N. Uversky ◽  
Ian S. Millett ◽  
Ritu Khurana ◽  
Sebastian Doniach ◽  
...  
Keyword(s):  
Light Chain ◽  
Amyloid Fibril ◽  
Conformational Stability ◽  
Fibril Formation ◽  
Immunoglobulin Light Chain ◽  
Amyloid Fibril Formation ◽  
Kinetics Of ◽  
Association State

Early Kinetics of Amyloid Fibril Formation Reveals Conformational Reorganisation of Initial Aggregates

2007 ◽  
Vol 366 (4) ◽  
pp. 1351-1363 ◽  
Author(s):  
N. Cerdà-Costa ◽  
A. Esteras-Chopo ◽  
F.X. Avilés ◽  
L. Serrano ◽  
V. Villegas
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Kinetics Of

scholarly journals Investigation of the Mechanism of β-Amyloid Fibril Formation by Kinetic and Thermodynamic Analyses

Langmuir ◽  
2008 ◽  
Vol 24 (11) ◽  
pp. 5802-5808 ◽  
Author(s):  
Ming-Shen Lin ◽  
Liang-Yu Chen ◽  
Hui-Ting Tsai ◽  
Steven S.-S. Wang ◽  
Yung Chang ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Β Amyloid

scholarly journals Inhibition of Protein Aggregation by Several Antioxidants

2018 ◽  
Vol 2018 ◽  
pp. 1-12 ◽  
Author(s):  
Samra Hasanbašić ◽  
Alma Jahić ◽  
Selma Berbić ◽  
Magda Tušek Žnidarič ◽  
Eva Žerovnik
Keyword(s):  
Vitamin C ◽  
Protein Aggregation ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Transmission Electron ◽  
Tht Fluorescence ◽  
Shared Property ◽  
High Concentrations ◽  
Kinetics Of

Amyloid fibril formation is a shared property of all proteins; therefore, model proteins can be used to study this process. We measured protein aggregation of the model amyloid-forming protein stefin B in the presence and absence of several antioxidants. Amyloid fibril formation by stefin B was routinely induced at pH 5 and 10% TFE, at room temperature. The effects of antioxidants NAC, vitamin C, vitamin E, and the three polyphenols resveratrol, quercetin, and curcumin on the kinetics of fibril formation were followed using ThT fluorescence. Concomitantly, the morphology and amount of the aggregates and fibrils were checked by transmission electron microscopy (TEM). The concentration of the antioxidants was varied, and it was observed that different modes of action apply at low or high concentrations relative to the binding constant. In order to obtain more insight into the possible mode of binding, docking of NAC, vitamin C, and all three polyphenols was done to the monomeric form of stefin B.

A Multimeric Quinacrine Conjugate as a Potential Inhibitor of Alzheimer's β-Amyloid Fibril Formation

ChemBioChem ◽  
2008 ◽  
Vol 9 (6) ◽  
pp. 952-963 ◽  
Author(s):  
Gunnar T. Dolphin ◽  
Sabine Chierici ◽  
Myriam Ouberai ◽  
Pascal Dumy ◽  
Julian Garcia
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Potential Inhibitor ◽  
Amyloid Fibril Formation ◽  
Β Amyloid

Cerebrospinal fluid of Alzheimer patients promotes β-amyloid fibril formation in vitro

2005 ◽  
Vol 20 (2) ◽  
pp. 233-240 ◽  
Author(s):  
Kenjiro Ono ◽  
Moeko Noguchi ◽  
Yasuko Matsumoto ◽  
Daisuke Yanase ◽  
Kazuo Iwasa ◽  
...  
Keyword(s):  
Cerebrospinal Fluid ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Β Amyloid

scholarly journals Common structural features determine the effectiveness of carvedilol, daunomycin and rolitetracycline as inhibitors of Alzheimer β-amyloid fibril formation

1999 ◽  
Vol 343 (2) ◽  
pp. 419 ◽  
Author(s):  
David R. HOWLETT ◽  
Ashley R. GEORGE ◽  
Davina E. OWEN ◽  
Robin V. WARD ◽  
Roger E. MARKWELL
Keyword(s):  
Amyloid Fibril ◽  
Structural Features ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Β Amyloid
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