Carbon nanotubes prevent 2,2,2 trifluoroethanol induced aggregation of protein

Ghule, Anil V.; Kathir, Karuppanan Muthusamy; Kumar, Thallapuranam Krishnaswamy Suresh; Tzing, Shin‐Hwa; Chang, Jia-Yaw; Yu, Chin; Ling, Yong‐Chien

doi:10.1016/j.carbon.2007.03.043

Cited by 33 publications

(42 citation statements)

References 8 publications

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“…The difference between the total free energy, DG, of the fibril and the sum of all contributions from individual Ab chains gives rise to a stabilization free energy of À389.5 for the wt, which is significantly reduced in the type III complex to À322. 8 in between the amine groups of adjacent K28 X as well as K28 X+1 residues, the above-mentioned salt bridge may also be regarded an inter-strand one (compare for example opinions in ref. 4 with those in ref.…”

Section: Alters Key-interactions In the Structure Of The Wt Ab Pmentioning

confidence: 98%

“…fullerene (C 60 ) and carbon nanotubes (CNTs), that showed remarkable activity in the context of AD. [8][9][10][11] Recent drug discovery efforts focusing on the aggregation stage of Ab peptides have mainly been based on two strategies: (i) the inhibition of initial Ab nucleation and oligomer formation, [12][13][14][15] and (ii) the disintegration of plaques and disruption of fibril structure. 16,17 A very recent report demonstrated the successful application of structure-based in silico design of peptidic inhibitors blocking amyloid fibril formation.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Amyloid-β fibril disruption by C60—molecular guidance for rational drug design

Andújar

Lugli

Höfinger

et al. 2012

Phys. Chem. Chem. Phys.

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The WHO has listed Alzheimer's disease among the major neurological disorders with an estimated 35 million people affected worldwide. Amyloid-β is mostly believed to be the causative factor in Alzheimer's disease and the severity of the disease correlates with the tendency of amyloid-β to form aggregation patterns-plaques. Lacking effective medication, the identification of any underlying mechanistic principles regarding plaque formation appears to be crucial. Here we carry out computer simulations to study the effect of C60 on structure and stability of an idealised pentameric construct of amyloid-β units (a model fibril). A binding site on top of the structurally ordered stack of β-sheets is identified that triggers structural alterations at the turn region of the hook-like β-sheet assembly. Significant structural alterations are: (i) the destruction of regular helical twist, (ii) the loss of a stabilizing salt bridge and (iii) the loss of a stabilizing hydrophobic interaction close to the turn. Consequently, the main effect of C60 is the induction of sizable destabilization in native fibril structure. These structural insights may serve as a molecular guide for further rational drug design of effective inhibitors targeting fibril formation in Alzheimer's disease.

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Section: Alters Key-interactions In the Structure Of The Wt Ab Pmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Amyloid-β fibril disruption by C60—molecular guidance for rational drug design

Andújar

Lugli

Höfinger

et al. 2012

Phys. Chem. Chem. Phys.

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“…2, 3 Alzheimer's disease (AD) 3 is one of the best-known amyloid disorder diseases, and it is characterized by the aggregation of amyloid-b (Ab) proteins in the brain. [5][6][7][8][9] In recent decades, nanomaterials, especially nanoparticles, have been increasingly applied in biomedicine for therapeutic and diagnostic purposes. [5][6][7][8][9] In recent decades, nanomaterials, especially nanoparticles, have been increasingly applied in biomedicine for therapeutic and diagnostic purposes.…”

Section: Introductionmentioning

confidence: 99%

Influence of Au nanoparticles on the aggregation of amyloid-β-(25–35) peptides

Wei

Yang

2013

Nanoscale

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The influence of Au nanoparticles (Au NPs) on the aggregation of amyloid-β-(25-35) peptides (Aβ25-35) is investigated by atomic force microscopy and Thioflavin T fluorescence measurements. It is found that, without Au NPs, the Aβ25-35 peptides aggregate gradually from monomers and oligomers to long fibrils with the incubation time. In contrast, short protofibrils are formed quickly after Au NPs are added to the Aβ25-35 solution, which can be further aggregated to form short fibril bundles or even bundle conjunctions. To reveal the origin of Au NPs on the aggregation of Aβ25-35, electrostatic force microscopy and scanning Kelvin microscopy are employed to investigate the electrical properties of the Aβ25-35 fibrils with and without Au NPs. Due to the significant difference of the electrical properties between the Aβ25-35 fibrils and Au NPs, the locations of Au NPs inside the Aβ25-35 fibril bundles can be revealed and hence a possible influence mechanism of Au NPs on the aggregation of Aβ25-35 is suggested.

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“…CNT exhibit impressive potentials in many applications such as electrical interconnects, (Kreupl et al 2004;Li et al 2003) thermal interface materials, (Biercuk et al 2002;Liu et al 2004) high-performance fibers, (Koziol et al 2007;Vigolo et al 2000), environmental monitoring (Lee, Sun, and Ling 2009;Lee et al 2010), and health & biotechnology (Ghule et al 2007) so on. Although the theoretical intrinsic electrical, thermal, and mechanical properties of an individual CNT are extraordinary, synthesized CNTs in reality are far from being defectfree.…”

Section: Carbon Nanotube and Microwave Interactionmentioning

confidence: 99%