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

Cerebrospinal fluid inhibits Alzheimer ?-amyloid fibril formation in vitro

1993 ◽  
Vol 34 (4) ◽  
pp. 631-633 ◽  
Author(s):  
Thomas Wisniewski ◽  
Eduardo Castano ◽  
Jorge Ghiso ◽  
Blas Frangione
Keyword(s):  
Cerebrospinal Fluid ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

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

Apolipoprotein E and Antioxidants Have Different Mechanisms of Inhibiting Alzheimer's β-Amyloid Fibril Formation in Vitro†

Biochemistry ◽  
1998 ◽  
Vol 37 (51) ◽  
pp. 17882-17889 ◽  
Author(s):  
Hironobu Naiki ◽  
Kazuhiro Hasegawa ◽  
Itaru Yamaguchi ◽  
Hideki Nakamura ◽  
Fumitake Gejyo ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Β Amyloid

P4-023: Cerebrospinal fluid of Alzheimer patients promotes beta-amyloid fibril formation in vitro

2006 ◽  
Vol 2 ◽  
pp. S520-S520
Author(s):  
Kenjiro Ono ◽  
Moeko Noguchi ◽  
Yasuko Matsumoto ◽  
Daisuke Yanase ◽  
Kazuo Iwasa ◽  
...  
Keyword(s):  
Cerebrospinal Fluid ◽  
Amyloid Fibril ◽  
Beta Amyloid ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

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.

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