Insights into the mechanism of methionine oxidation catalyzed by metal (Cu2+, Zn2+, and Fe3+)-Amyloid beta (Aβ) peptide complexes: A computational study

2009 ◽  
Vol 30 (9) ◽  
pp. 1405-1413 ◽  
Author(s):  
Arghya Barman ◽  
Woody Taves ◽  
Rajeev Prabhakar
Keyword(s):  
Amyloid Beta ◽  
Computational Study ◽  
Methionine Oxidation ◽  
Aβ Peptide ◽  
Peptide Complexes

scholarly journals Methionine Oxidation Changes the Mechanism of Aβ Peptide Binding to the DMPC Bilayer

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Christopher Lockhart ◽  
Amy K. Smith ◽  
Dmitri K. Klimov
Keyword(s):  
Peptide Binding ◽  
Methionine Oxidation ◽  
Aβ Peptide ◽  
Dmpc Bilayer

scholarly journals Efficient extraction of intact HSA-Aβ peptide complexes from sera: Toward albuminome biomarker identification

Talanta ◽  
2020 ◽  
Vol 216 ◽  
pp. 121002 ◽  
Author(s):  
Emilie Rossi ◽  
N. Thuy Tran ◽  
Christophe Hirtz ◽  
Sylvain Lehmann ◽  
Myriam Taverna
Keyword(s):  
Aβ Peptide ◽  
Biomarker Identification ◽  
Efficient Extraction ◽  
Peptide Complexes

Electrochemistry of Alzheimer Disease Amyloid Beta Peptides

2018 ◽  
Vol 25 (33) ◽  
pp. 4066-4083 ◽  
Author(s):  
Ana-Maria Chiorcea-Paquim ◽  
Teodor Adrian Enache ◽  
Ana Maria Oliveira-Brett
Keyword(s):  
Amino Acid ◽  
Amyloid Beta ◽  
Biological Fluids ◽  
Electron Transfer Reaction ◽  
Random Coil ◽  
Sequence Length ◽  
Dependent Manner ◽  
Aβ Peptide ◽  
Aβ Peptides ◽  
Α Helix

Alzheimer’s disease (AD) is a widespread form of dementia that is estimated to affect 44.4 million people worldwide. AD pathology is closely related to the accumulation of amyloid beta (Aβ) peptides in fibrils and plagues, the small oligomeric intermediate species formed during the Aβ peptides aggregation presenting the highest neurotoxicity. This review discusses the recent advances on the Aβ peptides electrochemical characterization. The Aβ peptides oxidation at a glassy carbon electrode occurs in one or two steps, depending on the amino acid sequence, length and content. The first electron transfer reaction corresponds to the tyrosine Tyr10 amino acid residue oxidation, and the second to all three histidine (His6, His13 and His14) and one methionine (Met35) amino acid residues. The Aβ peptides aggregation and amyloid fibril formation are electrochemically detected via the electroactive amino acids oxidation peak currents decrease that occurs in a time dependent manner. The Aβ peptides redox behaviour is correlated with changes in the adsorption morphology from initially random coiled structures, corresponding to the Aβ peptide monomers in random coil or in α-helix conformations, to aggregates, protofibrils and two types of fibrils, corresponding to the Aβ peptides in a β-sheet configuration, observed by atomic force microscopy. Electrochemical studies of Aβ peptides aggregation, mediated by the interaction with metal ions, particularly zinc, copper and iron, and different methodologies concerning the detection of Aβ peptide biomarkers of AD in biological fluids, using electrochemical biosensors, are also discussed.

Engineered non-fluorescent Affibody molecules facilitate studies of the amyloid-beta (Aβ) peptide in monomeric form: Low pH was found to reduce Aβ/Cu(II) binding affinity

2013 ◽  
Vol 120 ◽  
pp. 18-23 ◽  
Author(s):  
Joel Lindgren ◽  
Patrik Segerfeldt ◽  
Sabrina B. Sholts ◽  
Astrid Gräslund ◽  
Amelie Eriksson Karlström ◽  
...  
Keyword(s):  
Binding Affinity ◽  
Amyloid Beta ◽  
Low Ph ◽  
Aβ Peptide ◽  
Monomeric Form ◽  
Affibody Molecules

On the propagation of the OH radical produced by Cu-amyloid beta peptide model complexes. Insight from molecular modelling

Metallomics ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 1765-1780
Author(s):  
Federica Arrigoni ◽  
Fabio Rizza ◽  
Renata Tisi ◽  
Luca De Gioia ◽  
Giuseppe Zampella ◽  
...  
Keyword(s):  
Amyloid Beta ◽  
Molecular Modelling ◽  
Amyloid Beta Peptide ◽  
Side Chains ◽  
Oh Radical ◽  
Ros Production ◽  
Aβ Peptide ◽  
Model Complexes ◽  
Beta Peptide ◽  
Amyloid Aβ

Alzheimer's disease involves an anomalous interaction of copper with the amyloid Aβ peptide, inducing ROS production. The propagation of the OH radical toward Aβ side chains is investigated by molecular modelling.

scholarly journals Accumulation of Innate Amyloid Beta Peptide in Glioblastoma Tumors

2019 ◽  
Vol 20 (10) ◽  
pp. 2482 ◽  
Author(s):  
Lilia Y. Kucheryavykh ◽  
Jescelica Ortiz-Rivera ◽  
Yuriy V. Kucheryavykh ◽  
Astrid Zayas-Santiago ◽  
Amanda Diaz-Garcia ◽  
...  
Keyword(s):  
Blood Vessels ◽  
Amyloid Beta ◽  
Glioma Cells ◽  
Amyloid Beta Peptide ◽  
Enzyme Linked Immunosorbent Assay ◽  
Aβ Peptide ◽  
Brain Areas ◽  
Aβ Peptides ◽  
Beta Peptide ◽  
Glioma Tumors

Immunostaining with specific antibodies has shown that innate amyloid beta (Aβ) is accumulated naturally in glioma tumors and nearby blood vessels in a mouse model of glioma. In immunofluorescence images, Aβ peptide coincides with glioma cells, and enzyme-linked immunosorbent assay (ELISA) have shown that Aβ peptide is enriched in the membrane protein fraction of tumor cells. ELISAs have also confirmed that the Aβ(1–40) peptide is enriched in glioma tumor areas relative to healthy brain areas. Thioflavin staining revealed that at least some amyloid is present in glioma tumors in aggregated forms. We may suggest that the presence of aggregated amyloid in glioma tumors together with the presence of Aβ immunofluorescence coinciding with glioma cells and the nearby vasculature imply that the source of Aβ peptides in glioma can be systemic Aβ from blood vessels, but this question remains unresolved and needs additional studies.

scholarly journals Computational Study of Natural Compounds for the Clearance of Amyloid-Βeta: A Potential Therapeutic Management Strategy for Alzheimer’s Disease

Molecules ◽  
2019 ◽  
Vol 24 (18) ◽  
pp. 3233 ◽  
Author(s):  
Syed Sayeed Ahmad ◽  
Haroon Khan ◽  
Syed Mohd. Danish Rizvi ◽  
Siddique Akber Ansari ◽  
Riaz Ullah ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Computational Study ◽  
Senile Plaques ◽  
Natural Compounds ◽  
Positive Control ◽  
Aβ Peptide ◽  
Protein Protein Interaction ◽  
Lead Compounds ◽  
Glycation End Products

Alzheimer’s disease (AD) is a widespread dynamic neurodegenerative malady. Its etiology is still not clear. One of the foremost pathological features is the extracellular deposits of Amyloid-beta (Aβ) peptides in senile plaques. The interaction of Aβ and the receptor for advanced glycation end products at the blood-brain barrier is also observed in AD, which not only causes the neurovascular anxiety and articulation of proinflammatory cytokines, but also directs reduction of cerebral bloodstream by upgrading the emission of endothelin-1 to induce vasoconstriction. In this process, RAGE is deemed responsible for the influx of Aβ into the brain through BBB. In the current study, we predicted the interaction potential of the natural compounds vincamine, ajmalicine and emetine with the Aβ peptide concerned in the treatment of AD against the standard control, curcumin, to validate the Aβ peptide–compounds results. Protein-protein interaction studies have also been carried out to see their potential to inhibit the binding process of Aβ and RAGE. Moreover, the current study verifies that ligands are more capable inhibitors of a selected target compared to positive control with reference to ΔG values. The inhibition of Aβ and its interaction with RAGE may be valuable in proposing the next round of lead compounds for effective Alzheimer’s disease treatment.

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