scholarly journals Prediction of fibril formation by early-stage amyloid peptide aggregation

2020 ◽  
Vol 10 (2) ◽  
pp. 194-199 ◽  
Author(s):  
Jiaojiao Hu ◽  
Huiyong Sun ◽  
Haiping Hao ◽  
Qiuling Zheng
Keyword(s):  
Early Stage ◽  
Fibril Formation ◽  
Amyloid Peptide ◽  
Peptide Aggregation

scholarly journals Anti-Aggregation Property of Allicin by In Vitro and Molecular Docking Studies

2019 ◽  
Vol 13 ◽  
pp. 117906951986618 ◽  
Author(s):  
Suresh Kumar ◽  
Shivani Kumar ◽  
Heera Ram
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Molecular Docking ◽  
Molecular Interaction ◽  
Fibril Formation ◽  
Amyloid Peptide ◽  
Peptide Aggregation ◽  
Aβ Peptide ◽  
In Silico Studies

Amyloidogenesis is the process in which amyloid beta (Aβ) peptide aggregation results in plaque formation in central nervous system (CNS) are associated with many neurological diseases such as Alzheimer’s disease. The peptide aggregation initiated from peptide monomers results in formation of dimers, tetramers, fibrils, and protofibrils. The ability of allicin, a lipid-soluble volatile organosulfur biological compound, present in freshly crushed garlic ( Allium sativum L.) to inhibit fibril formation by the Aβ peptide in vitro was investigated in the present study. Inhibition of fibrillogenesis was measured by a Thioflavin T (ThT) fluorescence assay and visualized by transmission electron microscopy (TEM). The molecular interaction between allicin and Aβ peptide was also demonstrated by in silico studies. The results show that allicin strongly inhibited Aβ fibrils by 97% at 300 µM, compared with control (Aβ only) ( P < .001). These results were further validated by visual of fibril formation by transmission microscopy and molecular interaction of amyloid peptide with allicin by molecular docking. Aβ forms favourable hydrophobic interaction with Ile32, Met35, Val36, and Val39, and oxygen of allicin forms hydrogen bond with the amino acid residue Lys28. Allicin anti-amyloidogenic property suggests that this naturally occurring compound may have potential to ameliorate and prevent Alzheimer’s disease.

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

Graphene oxide-iron oxide nanocomposite as an inhibitor of Aβ 42 amyloid peptide aggregation

2017 ◽  
Vol 159 ◽  
pp. 540-545 ◽  
Author(s):  
Israr Ahmad ◽  
Anbu Mozhi ◽  
Lin Yang ◽  
Qiusen Han ◽  
Xingjie Liang ◽  
...  
Keyword(s):  
Graphene Oxide ◽  
Iron Oxide ◽  
Amyloid Peptide ◽  
Peptide Aggregation

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 Inhibition of Prion Amyloid Peptide Fibril Formation by Peroxovanadium Complexes

2016 ◽  
Vol 32 (7) ◽  
pp. 1810-1818
Author(s):  
Bao-Hong ZHANG ◽  
◽  
Guo-Sheng HU ◽  
Deng-Sen ZHU ◽  
Wen-Ji WANG ◽  
...  
Keyword(s):  
Fibril Formation ◽  
Amyloid Peptide

Impact of nanoparticles on amyloid peptide and protein aggregation: a review with a focus on gold nanoparticles

Nanoscale ◽  
2018 ◽  
Vol 10 (45) ◽  
pp. 20894-20913 ◽  
Author(s):  
Torsten John ◽  
Anika Gladytz ◽  
Clemens Kubeil ◽  
Lisandra L. Martin ◽  
Herre Jelger Risselada ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Protein Aggregation ◽  
Amyloid Peptide ◽  
Peptide Aggregation

The accelerating and inhibiting effects of nanoparticles on amyloid peptide aggregation are discussed for varying nanoparticle and peptide properties in the context of recent studies.

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