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 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.

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

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

scholarly journals Thermodynamics of β-amyloid fibril formation

2004 ◽  
Vol 120 (17) ◽  
pp. 8307-8317 ◽  
Author(s):  
G. Tiana ◽  
F. Simona ◽  
R. A. Broglia ◽  
G. Colombo
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Β Amyloid

Blood-borne factors inhibit Alzheimer's β-amyloid fibril formation in vitro

2006 ◽  
Vol 202 (1) ◽  
pp. 125-132 ◽  
Author(s):  
K ONO ◽  
M NOGUCHISHINOHARA ◽  
M SAMURAKI ◽  
Y MATSUMOTO ◽  
D YANASE ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Β Amyloid

Interaction between Aβ(1−42) and Aβ(1−40) in Alzheimer's β-Amyloid Fibril Formation in Vitro†

Biochemistry ◽  
1999 ◽  
Vol 38 (47) ◽  
pp. 15514-15521 ◽  
Author(s):  
Kazuhiro Hasegawa ◽  
Itaru Yamaguchi ◽  
Saburou Omata ◽  
Fumitake Gejyo ◽  
Hironobu Naiki
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Β Amyloid
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