Inhibition of Alzheimer's amyloid-beta aggregation in-vitro by carbenoxolone: Insight into mechanism of action

  title={Inhibition of Alzheimer's amyloid-beta aggregation in-vitro by carbenoxolone: Insight into mechanism of action},
  author={Sheetal Sharma and Bimla Nehru and Avneet Saini},
  journal={Neurochemistry International},
Bleomycin modulates amyloid aggregation in β-amyloid and hIAPP
Combined results from drug repurposing and replica exchange molecular dynamics simulations demonstrate that BLM binds to the β-sheet region considered a hotspot for amyloid fibrils of Aβ and hIAPP, and for the first time, this study shows that BLM is a dual inhibitor of A α-sheet aggregation.
Carbenoxolone Reverses the Amyloid Beta 1–42 Oligomer–Induced Oxidative Damage and Anxiety-Related Behavior in Rats
Carbenoxolone prevents the Aβ 42 oligomer–induced oxidative damage and anxiety-like behavior partly by blocking the gap junction communication, which suggests that the therapeutic potential of Cbx may be explored in the progression of AD.
Biological and methodological complexities of beta‐amyloid peptide: Implications for Alzheimer’s disease research
Although controversial, the amyloid cascade hypothesis remains central to the Alzheimer's disease (AD) field and posits amyloid‐beta (Aβ) as the central factor initiating disease onset. In recent
Unconjugated PLGA nanoparticles attenuate temperature-dependent β-amyloid aggregation and protect neurons against toxicity: implications for Alzheimer’s disease pathology
It is suggested that PLGA nanoparticles can inhibit Aβ aggregation and trigger disassembly of Aβ aggregates at temperatures outside the physiological range and can protect neurons against Aβ-mediated toxicity thus validating its unique therapeutic potential in the treatment of AD pathology.
Self-assembly of N-terminal Alzheimer's β-amyloid and its inhibition.
  • G. Prasanna, P. Jing
  • Chemistry, Biology
    Biochemical and biophysical research communications
  • 2020
Recent advances in the design and applications of amyloid-β peptide aggregation inhibitors for Alzheimer’s disease therapy
A comprehensive view of the challenges in AD therapy and pathophysiology is provided and currently known compounds that can inhibit amyloid-β (Aβ) aggregation and their potential role in advancing current AD treatments are discussed.


Vitamin k3 inhibits protein aggregation: Implication in the treatment of amyloid diseases
It is demonstrated that vitamin k3 significantly inhibits fibril formation as well as the inhibitory effect is dose dependent manner, paving the way for discovery of other small molecules that may exert similar effect against amyloid formation and its associated neurodegenerative diseases.
New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease.
The inhibitory properties of the compounds presented suggest a new class of small molecules that could serve as a scaffold for the design of more efficient inhibitors of Abeta amyloidogenesis in vivo.
Comparative docking and ADMET study of some curcumin derivatives and herbal congeners targeting β-amyloid
Principal descriptors as well as absorption, distribution, metabolism, excretion and toxicity (ADMET) properties for these compounds were predicted, and were found satisfactory, and was found satisfactory.
Inhibition of amyloid fibril formation and cytotoxicity by a chemical analog of Curcumin as a stable inhibitor.
Computational Design of New Peptide Inhibitors for Amyloid Beta (Aβ) Aggregation in Alzheimer's Disease: Application of a Novel Methodology
A peptide, experimentally proven to bind Aβ40 fibrils at the GxMxG motif, was mutated by a novel methodology that systematically replaces amino acids with residues that share similar chemical characteristics and subsequently assesses the energetic favorability of these mutations by docking.
Quantifying amyloid beta-peptide (Abeta) aggregation using the Congo red-Abeta (CR-abeta) spectrophotometric assay.
The CR-Abeta method is equally simple and retains the advantages of speed and lack of necessity for specialized instrumentation or expensive/radioactive reagents, and can directly provide quantitation of aggregated Abeta in absolute terms.
Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid
A molecular-level examination of sequence-specific secondary structures and supramolecular structures of a neurotoxic amyloid intermediate of the 40-residue β-amyloid peptide involved in Alzheimer's disease shows that Iβ shows higher toxicity than the fibril, indicating that the β-sheet formation may trigger neurotoxicity.
Quantifying Amyloid β-Peptide (Aβ) Aggregation Using the Congo Red-Aβ (CR–Aβ) Spectrophotometric Assay
Abstract Congo red (CR) is a histologic dye that binds to many amyloid proteins because of their extensive β-sheet structure. The absorbance spectrum of the dye changes upon binding to amyloid. This