Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR†

Biochemistry ◽  
2000 ◽  
Vol 39 (45) ◽  
pp. 13748-13759 ◽  
Author(s):  
John J. Balbach ◽  
Yoshitaka Ishii ◽  
Oleg N. Antzutkin ◽  
Richard D. Leapman ◽  
Nancy W. Rizzo ◽  
...  
Keyword(s):  
Solid State ◽  
Structural Characterization ◽  
Solid State Nmr ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Peptide ◽  
Amyloid Fibril Formation ◽  
Β Amyloid ◽  
Β Amyloid Peptide

Solid State NMR Reveals a pH-dependent Antiparallel β-Sheet Registry in Fibrils Formed by a β-Amyloid Peptide

2004 ◽  
Vol 335 (1) ◽  
pp. 247-260 ◽  
Author(s):  
A.T. Petkova ◽  
G. Buntkowsky ◽  
F. Dyda ◽  
R.D. Leapman ◽  
W.-M. Yau ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Amyloid Peptide ◽  
Β Amyloid ◽  
Ph Dependent ◽  
Β Amyloid Peptide ◽  
Β Sheet

Inhibitors of Fibril Formation and Cytotoxicity of β-Amyloid Peptide Composed of KLVFF Recognition Element and Flexible Hydrophilic Disrupting Element

2002 ◽  
Vol 290 (1) ◽  
pp. 121-124 ◽  
Author(s):  
Ken-ichi Watanabe ◽  
Kazuhiko Nakamura ◽  
Shingo Akikusa ◽  
Tomoko Okada ◽  
Masato Kodaka ◽  
...  
Keyword(s):  
Fibril Formation ◽  
Amyloid Peptide ◽  
Recognition Element ◽  
Β Amyloid ◽  
Β Amyloid Peptide

scholarly journals Inhibition of fibril formation in β-amyloid peptide by a novel series of benzofurans

1999 ◽  
Vol 340 (1) ◽  
pp. 283 ◽  
Author(s):  
David R. HOWLETT ◽  
Amanda E. PERRY ◽  
Fiona GODFREY ◽  
Jane E. SWATTON ◽  
Kevin H. JENNINGS ◽  
...  
Keyword(s):  
Fibril Formation ◽  
Amyloid Peptide ◽  
Β Amyloid ◽  
Β Amyloid Peptide

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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