Peptide–surfactant interactions: Consequences for the amyloid-beta structure

2012 ◽  
Vol 420 (1) ◽  
pp. 136-140 ◽  
Author(s):  
Sandra Rocha ◽  
Joana A. Loureiro ◽  
Gerald Brezesinski ◽  
Maria do Carmo Pereira
Keyword(s):  
Amyloid Beta ◽  
Surfactant Interactions ◽  
Beta Structure

Hydrophobic tail length plays a pivotal role in amyloid beta (25-35) fibril-surfactant interactions

2016 ◽  
Vol 84 (9) ◽  
pp. 1213-1223 ◽  
Author(s):  
Sudipta Bag ◽  
Susmitnarayan Chaudhury ◽  
Dibyendu Pramanik ◽  
Sunando DasGupta ◽  
Swagata Dasgupta
Keyword(s):  
Amyloid Beta ◽  
Tail Length ◽  
Pivotal Role ◽  
Surfactant Interactions ◽  
Hydrophobic Tail

scholarly journals Spectroscopic investigation of the effect of polyphenolic compounds on the amyloid-[beta] protein

2017 ◽  
Author(s):  
◽  
Brittany L. Hagenhoff
Keyword(s):  
Amyloid Beta ◽  
Rosmarinic Acid ◽  
Nordihydroguaiaretic Acid ◽  
Polyphenolic Compounds ◽  
Beta Sheet ◽  
Amyloid Beta Protein ◽  
Final State ◽  
Deep Ultraviolet ◽  
Beta Structure ◽  
Ultraviolet Resonance Raman

Aggregation of the amyloid-[beta] (A[beta]) protein is associated with the development of Alzheimer's disease. A[beta] is a 39-43 residue cleavage product of the amyloid precursor protein (APP). A[beta] aggregates to produce insoluble plaques in the brain, which are composed of cross [beta]-sheet structured fibrils. Various polyphenolic compounds, both naturally occurring and synthetic, have been shown to interfere with A[beta] aggregation. To evaluate the ability of specific polyphenols to prevent A[beta] aggregation, this investigation utilized nordihydroguaiaretic acid, curcumin, rosmarinic acid, resveratrol, piceatannol, and diethylstilbestrol. These polyphenols differ in the number of ring substituents and the atom linker between the rings. The interaction of A[beta] with the polyphenolic compounds was analyzed using circular dichroism (CD) and deep ultraviolet resonance Raman (dUVRR) spectroscopies. The polyphenols diethylstilbestrol, resveratrol, and piceatannol have increasing numbers of hydroxyl substituents on their rings, having two, three, and four respectively. It was found that with increasing number of hydroxyl ring substituents, the protein remained predominantly disordered and prevented formation of [beta]-structure in the protein and aided in the destabilization of pre-formed A[beta] fibrils. Decreasing the number of hydroxyl substituents increases the likelihood of [beta]-sheet formation, prevented destabilization of pre-formed A[beta] fibrils, and induced loss of stability of the protein. The polyphenols nordihydroguaiaretic acid, curcumin, and rosmarinic acid have increasing polarity respectively in the chain linker between the phenolic rings. Each of these polyphenols have four ring substituents and have four to six atoms in their chain linker. It was found that with increasing the polarity of the linker, the protein had a greater tendency to form a [beta]-structure, however pre-formed A[beta] fibrils were destabilized efficiently by all three polyphenols. Though a nonpolar chain linker pushed fibrillar protein toward a more disordered structure initially, the final state was similar regardless of added polyphenol.

scholarly journals Amyloid beta: structure, biology and structure-based therapeutic development

2017 ◽  
Vol 38 (9) ◽  
pp. 1205-1235 ◽  
Author(s):  
Guo-fang Chen ◽  
Ting-hai Xu ◽  
Yan Yan ◽  
Yu-ren Zhou ◽  
Yi Jiang ◽  
...  
Keyword(s):  
Amyloid Beta ◽  
Therapeutic Development ◽  
Beta Structure

Crystalline order to a resolution of 4.7 A in the sheath of Methanospirilium hungatii: A cross-beta structure

1984 ◽  
Vol 42 ◽  
pp. 214-215
Author(s):  
Murray Stewart ◽  
T.J. Beveridge ◽  
D. Sprott
Keyword(s):  
Cell Wall ◽  
Single Layer ◽  
Uranyl Acetate ◽  
Optical Diffraction ◽  
Tube Axis ◽  
Basic Subunit ◽  
Beta Structure ◽  
Diffraction Patterns ◽  
Protein Treatment ◽  
General Appearance

The archaebacterium Methanospirillum hungatii has a sheath as part of its cell wall which is composed mainly of protein. Treatment with dithiothreitol or NaOH released the intact sheaths and electron micrographs of this material negatively stained with uranyl acetate showed flattened hollow tubes, about 0.5 μm diameter and several microns long, in which the patterns from the top and bottom were superimposed. Single layers, derived from broken tubes, were also seen and were more simply analysed. Figure 1 shows the general appearance of a single layer. There was a faint axial periodicity at 28.5 A, which was stronger at irregular multiples of 28.5 A (3 and 4 times were most common), and fine striations were also seen at about 3° to the tube axis. Low angle electron diffraction patterns (not shown) and optical diffraction patterns (Fig. 2) from these layers showed a complex meridian (as a result of the irregular nature of the repeat along the tube axis) which showed a clear maximum at 28.5 A, consistent with the basic subunit spacing.

Proteolytic processing of the amyloid-beta protein precursor of Alzheimer's disease

2002 ◽  
Vol 38 ◽  
pp. 37-49 ◽  
Author(s):  
Janelle Nunan ◽  
David H Small
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Beta ◽  
Alternative Pathway ◽  
Protein A ◽  
Proteolytic Processing ◽  
Gamma Secretase ◽  
Amyloid Beta Protein ◽  
Protein Precursor ◽  
Amyloid Beta Protein Precursor

The proteolytic processing of the amyloid-beta protein precursor plays a key role in the development of Alzheimer's disease. Cleavage of the amyloid-beta protein precursor may occur via two pathways, both of which involve the action of proteases called secretases. One pathway, involving beta- and gamma-secretase, liberates amyloid-beta protein, a protein associated with the neurodegeneration seen in Alzheimer's disease. The alternative pathway, involving alpha-secretase, precludes amyloid-beta protein formation. In this review, we describe the progress that has been made in identifying the secretases and their potential as therapeutic targets in the treatment or prevention of Alzheimer's disease.

Mitochondrial failure precedes amyloid beta plaques deposition in APP transgenic mice

2005 ◽  
Vol 38 (05) ◽  
Author(s):  
A Eckert ◽  
I Scherping ◽  
A Bonert ◽  
S Hauptmann ◽  
F Müller-Spahn ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Amyloid Beta
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