Hemin is able to disaggregate lysozyme amyloid fibrils into monomers

Sonavane, Sumalata; Haider, Syeda Zehra; Kumar, Anil; Ahmad, Basir

doi:10.1016/j.bbapap.2017.07.017

Cited by 17 publications

(10 citation statements)

References 38 publications

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“…These early perturbations that fragment a few H-bonds occur in the core of the fibrils and then propagate to the fibril extremities resulting in unstructured expanded oligomers. In this context, this mechanism is quite different from that obtained by using other methods such as ultrasound, drugs, or graphene nanosheet, where the peptides on the surface of the fibril are detached first. ,,, …”

Section: Discussionmentioning

confidence: 79%

Infrared Laser-Induced Amyloid Fibril Dissociation: A Joint Experimental/Theoretical Study on the GNNQQNY Peptide

et al. 2020

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Neurodegenerative diseases are usually characterized by plaques made of well-ordered aggregates of distinct amyloid proteins. Dissociating these very stable amyloid plaques is a critical clinical issue. In this study, we present a joint mid-infrared free electron laser experiment/non-equilibrium molecular dynamics simulation to understand the dissociation process of a representative example GNNQQNY fibril. By tuning the laser frequency to the amide I band of the fibril, the resonance takes place and dissociation is occurred. The calculated and observed wide-angle X-ray scattering profiles and secondary structures before and after laser irradiation being identical, we can propose a dissociation mechanism with high confidence from our simulations. We find that dissociation starts in the core of the fibrils by fragmenting the intermolecular hydrogen bonds and separating the peptides and then propagates to the fibril extremities leading to the formation of unstructured expanded oligomers. We suggest that this should be a generic mechanism of the laser-induced dissociation of amyloid fibrils.

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Section: Discussionmentioning

confidence: 79%

Infrared Laser-Induced Amyloid Fibril Dissociation: A Joint Experimental/Theoretical Study on the GNNQQNY Peptide

et al. 2020

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“…where CD is in millidegree, n is the number of amino acid residues, 1 is the path length of the cell in cm, and Cp is the molar concentration of the protein ( Sonavane et al, 2017 ). The K2D2 ( Perez-Iratxeta and Andrade-Navarro, 2008 ) software was used, and further analysis of the data was done using CAPITO ( Wiedemann et al, 2013 ).…”

Section: Methodsmentioning

confidence: 99%

Ofloxacin as a Disruptor of Actin Aggresome “Hirano Bodies”: A Potential Repurposed Drug for the Treatment of Neurodegenerative Diseases

Pathak

Parkar

Tripathi

et al. 2020

Front. Aging Neurosci.

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There is a growing number of aging populations that are more prone to the prevalence of neuropathological disorders. Two major diseases that show a late onset of the symptoms include Alzheimer’s disorder (AD) and Parkinson’s disorder (PD), which are causing an unexpected social and economic impact on the families. A large number of researches in the last decade have focused upon the role of amyloid precursor protein, Aβ-plaque, and intraneuronal neurofibrillary tangles (tau-proteins). However, there is very few understanding of actin-associated paracrystalline structures formed in the hippocampus region of the brain and are called Hirano bodies. These actin-rich inclusion bodies are known to modulate the synaptic plasticity and employ conspicuous effects on long-term potentiation and paired-pulse paradigms. Since the currently known drugs have very little effect in controlling the progression of these diseases, there is a need to develop therapeutic agents, which can have improved efficacy and bioavailability, and can transport across the blood–brain barrier. Moreover, finding novel targets involving compound screening is both laborious and is an expensive process in itself followed by equally tedious Food and Drug Administration (FDA) approval exercise. Finding alternative functions to the already existing FDA-approved molecules for reversing the progression of age-related proteinopathies is of utmost importance. In the current study, we decipher the role of a broad-spectrum general antibiotic (Ofloxacin) on actin polymerization dynamics using various biophysical techniques like right-angle light scattering, dynamic light scattering, circular dichroism spectrometry, isothermal titration calorimetry, scanning electron microscopy, etc. We have also performed in silico docking studies to deduce a plausible mechanism of the drug binding to the actin. We report that actin gets disrupted upon binding to Ofloxacin in a concentration-dependent manner. We have inferred that Ofloxacin, when attached to a drug delivery system, can act as a good candidate for the treatment of neuropathological diseases.

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“…24 The far-UV CD spectrum of the HCM indicates the presence of mainly an extended b-sheet conformation, as revealed by the single negative band at 215-218 nm. 24,25 The far-UV CD data were also analysed by calculating Kuhn's g-value, which is the ratio of a sample's CD and absorbance. 26,27 The g-value is an intensive property independent of the path length and concentration of the protein.…”

Section: Characterization Of the Hydrogel Constituting Materials (Hcm)mentioning

confidence: 99%

The physical basis of fabrication of amyloid-based hydrogels by lysozyme

Kumari

Ahmad

2019

RSC Adv.

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Hemin is able to disaggregate lysozyme amyloid fibrils into monomers

Cited by 17 publications

References 38 publications

Infrared Laser-Induced Amyloid Fibril Dissociation: A Joint Experimental/Theoretical Study on the GNNQQNY Peptide

Infrared Laser-Induced Amyloid Fibril Dissociation: A Joint Experimental/Theoretical Study on the GNNQQNY Peptide

Ofloxacin as a Disruptor of Actin Aggresome “Hirano Bodies”: A Potential Repurposed Drug for the Treatment of Neurodegenerative Diseases

The physical basis of fabrication of amyloid-based hydrogels by lysozyme

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