Effect of nitroderivatives of fullerene C60 on amyloid fibrils of the brain Aβ(1–42) peptide and muscle X-protein

Bobylev, A. G.; Marsagishvili, L. G.; Shpagina, M. D.; Романова, В. С.; Kotelnikova, R. A.; Podlubnaya, Z. A.

doi:10.1134/s0006350910030024

Cited by 9 publications

(6 citation statements)

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“…The correlation between DG bind and the number of carbon atoms of fullerenes is 0.997 and 0.909 for 5Ab 17-42 and 12Ab 9-40 , respectively. The strong binding of C60 to both targets is qualitatively consistent with experiments [38][39][40][41][42] and prior simulations. 43 The binding affinity of C36 and C60 for 12Ab 9-40 is compatible to that of curcumin.…”

Section: Estimation Of Dgsupporting

confidence: 86%

“…39 More complicated derivatives of fullerenes such as (C60Cl(C 6 H 4 CH 2 C)Na), Na 4 [C60(OH) 30 ] and the complexes of fullerenes with polyvinylpyrrolidone were reported to have an inhibitory effect on Ab 1-42 . [40][41][42] Computationally, docking and molecular dynamics (MD) simulations 43 suggested that C60 preferentially binds to the turn region of the hook-like b-sheet, disrupting the Ab 1-42 fibril. However, the binding free energy of fullrenes to Ab fibrils was not estimated and the impact of fullerene size on binding affinity has not been studied either in silico or in vitro.…”

Section: Introductionmentioning

confidence: 99%

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Binding of fullerenes to amyloid beta fibrils: size matters

Huy¹,

Li²

2014

Phys. Chem. Chem. Phys.

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Binding affinity of fullerenes C20, C36, C60, C70 and C84 for amyloid beta fibrils is studied by docking and all-atom molecular dynamics simulations with the Amber force field and water model TIP3P. Using the molecular mechanic-Poisson Boltzmann surface area method one can demonstrate that the binding free energy linearly decreases with the number of carbon atoms of fullerene, i.e. the larger is the fullerene size, the higher is the binding affinity. Overall, fullerenes bind to Aβ9-40 fibrils stronger than to Aβ17-42. The number of water molecules trapped in the interior of 12Aβ9-40 fibrils was found to be lower than inside pentamer 5Aβ17-42. C60 destroys Aβ17-42 fibril structure to a greater extent compared to other fullerenes. Our study revealed that the van der Waals interaction dominates over the electrostatic interaction and non-polar residues of amyloid beta peptides play the significant role in interaction with fullerenes providing novel insight into the development of drug candidates against Alzheimer's disease.

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Section: Estimation Of Dgsupporting

confidence: 86%

Section: Introductionmentioning

confidence: 99%

Binding of fullerenes to amyloid beta fibrils: size matters

Huy¹,

Li²

2014

Phys. Chem. Chem. Phys.

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“…Earlier we have shown that fullerene C 60 and a number of its derivatives are capable of destroying amyloid fibrils of brain Aβ(1-42) peptide, participat ing in the pathogenesis of Alzheimer's disease, and also muscle X protein [17][18][19][20][21]. From the obtained results a conclusion has been made that fullerene C 60 and its derivatives may be regarded as potential anti amyloid preparations.…”

Section: Introductionmentioning

confidence: 83%

“…It has been shown that 1,2 (dimethoxymeth ano)fullerene is capable of inhibiting early stages of aggregation of Aβ(1-40) and Aβ (11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25) peptides of the brain, specifically binding with the central hydro phobic motif KLVFF (Lys Leu Val Phe Phe) of Aβ peptides [16].…”

Section: Introductionmentioning

confidence: 99%

Interaction of C60 fullerene-polyvinylpyrrolidone complex and brain Aβ(1–42)-peptide in vitro

et al. 2014

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Using a spectrophotometric method, changes occurring in solution containing brain Aβ(1-42) peptide, fullerene C 60 , and polyvinylpyrrolidone were analyzed. Using the Bent-French method, relative binding constants of fullerene C 60 with Aβ(1-42) peptide and polyvinylpyrrolidone with Aβ(1-42) peptide were determined. These data suggest that Aβ(1-42) peptide interacting with the C 60 fullerene-polyvinylpyr rolidone complex partially displaces polyvinylpyrrolidone and generates a new three molecular compound.

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“…It is known that [60]fullerene and many of its functional derivatives exhibit a range of promising neuroprotective activities. [2][3][4][5][6][7][8][9][10] It was also shown that some watersoluble carboxyfullerenes behave as superoxide dismutase mimics, and this activity correlates well with their neuroprotective efficacy. 11,12 Fullerene derivatives and their nanoclusters are also studied as promising drug carriers that can be used for delivering pharmaceutically important compounds to many therapeutic targets.…”

Section: Introductionmentioning

confidence: 99%