NDLI: Detection, inhibition and disintegration of amyloid fibrils: the role of optical probes and macrocyclic receptors

Please wait, while we are loading the content...

Unusual binding selectivity with non-selective homoditopic pillar[5]arene oxime: serendipitous discovery of a unique approach to heterobinuclear metalation in solution

Synthesis of spiro-oxoindoles through Pd-catalyzed remote C–H alkylation using α-diazocarbonyl compounds

Controlled formation of uniform nanoshells of manganese oxide and their potential in lithium ion batteries

Single gold nanowire electrodes and single Pt@Au nanowire electrodes: electrochemistry and applications

Iron catalyzed efficient synthesis of poly-functional primary amines via the direct use of ammonia

σ-Complexation as a strategy for designing copper-based light emitters

Nucleic acid detection using BRET-beacons based on bioluminescent protein–DNA hybrids

Surface chemistry of cadmium sulfide magic-sized clusters: a window into ligand-nanoparticle interactions

Efficient siRNA–peptide conjugation for specific targeted delivery into tumor cells

Measuring macromolecular crowding in cells through fluorescence anisotropy imaging with an AIE fluorogen

DNA display of folded RNA libraries enabling RNA-SELEX without reverse transcription

Correction: Enhanced resistive switching effect upon illumination in self-assembled NiWO₄ nano-nests

Inside back cover

Back cover

Chemical Communications Vol - 53 Issue - 9

Chemical Communications Vol - 53 Issue - 8

Chemical Communications Vol - 53 Issue - 7

Chemical Communications Vol - 53 Issue - 6

Chemical Communications Vol - 53 Issue - 5

Chemical Communications Vol - 53 Issue - 4

Chemical Communications Vol -49

Chemical Communications Vol -0

Detection, inhibition and disintegration of amyloid fibrils: the role of optical probes and macrocyclic receptors

Content Provider	Royal Society of Chemistry (RSC)
Author	Bhasikuttan, Achikanath C. Mohanty, Jyotirmayee
Copyright Year	2017
Abstract	Amyloid fibrils are formed by the aberrant aggregation of proteins into highly ordered β-sheet structures and are believed to be the root cause of several neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, Prion diseases, etc. and have been the subject of extensive biochemical, biophysical and clinical studies. Developing methods for the early detection of fibril formation using optical spectroscopic techniques and inhibition/disintegration of amyloid fibrils/plaques by introducing small molecules have been a major challenge to establish a clinically facile therapeutic intervention to combat these neurodegenerative diseases. This feature article provides an account of the recent reports from different research groups, including ours, on the optical detection, and inhibition/disintegration of mature fibrils using fluorescent probes and macrocyclic hosts such as cucurbiturils, calixarenes and cyclodextrins. Site specific or spectrally distinct fluorescence emission from a large number of fluorophores in a broad spectral region has been used to detect the fibrillation of different proteins/peptides, mainly insulin, α-synuclein, transthyretin, barstar, lysozyme, Aβ40 peptide, etc. On the one hand, while macrocyclic receptors modify the inter-protein interactions through molecular recognition of amino acid residues leading to the inhibition of amyloid fibrillation, on the other hand, one of the cavitands, p-sulfonatocalixarenes, has been demonstrated to cause the disintegration of mature fibrils, effectively through surface charge interactions, which destabilize the extended fibrillar structure into soluble or fine particles. Beneficially, the presence of extrinsic p-sulfonatocalix[4/6]arenes did not introduce any additional toxicity to the cell viability, which advocates its potential utility as a therapeutic for amyloidosis.
Starting Page	2789
Ending Page	2809
Page Count	21
File Format	HTM / HTML PDF
ISSN	13597345
Volume Number	53
Issue Number	19
Journal	Chemical Communications
DOI	10.1039/c6cc08727b
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Transthyretin Fluorescence Insulin Barstar Molecular recognition Prion Amyloid Amyloidosis Beta sheet Peptide Lysozyme Fibril
Content Type	Text
Resource Type	Article
Subject	Ceramics and Composites Chemistry Surfaces, Coatings and Films Materials Chemistry Metals and Alloys Electronic, Optical and Magnetic Materials Catalysis

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Formation and dissolution of hen egg white lysozyme amyloid fibrils in protic ionic liquids

The synergistic effect between KLVFF and self-assembly chaperones on both disaggregation of beta-amyloid fibrils and reducing consequent toxicity

Two distinct β-sheet fibrils from silk protein

Spectroscopic characterization of diverse amyloid fibrils in vitro by the fluorescent dye Nile red

Searching for the Best Transthyretin Aggregation Protocol to Study Amyloid Fibril Disruption

A multimodal, β-amyloid-targeted contrast agent

Use of a Mid-Infrared Free-Electron Laser (MIR-FEL) for Dissociation of the Amyloid Fibril Aggregates of a Peptide

Methionine oxidation of amyloid peptides by peroxovanadium complexes: inhibition of fibril formation through a distinct mechanism

Supramolecular photochirogenesis with functional amyloid superstructures

Detection, inhibition and disintegration of amyloid fibrils: the role of optical probes and macrocyclic receptors

Similar Documents

Formation and dissolution of hen egg white lysozyme amyloid fibrils in protic ionic liquids

The synergistic effect between KLVFF and self-assembly chaperones on both disaggregation of beta-amyloid fibrils and reducing consequent toxicity

Two distinct β-sheet fibrils from silk protein

Spectroscopic characterization of diverse amyloid fibrils in vitro by the fluorescent dye Nile red

Searching for the Best Transthyretin Aggregation Protocol to Study Amyloid Fibril Disruption

A multimodal, β-amyloid-targeted contrast agent

Use of a Mid-Infrared Free-Electron Laser (MIR-FEL) for Dissociation of the Amyloid Fibril Aggregates of a Peptide

Methionine oxidation of amyloid peptides by peroxovanadium complexes: inhibition of fibril formation through a distinct mechanism

Supramolecular photochirogenesis with functional amyloid superstructures

Detection, inhibition and disintegration of amyloid fibrils: the role of optical probes and macrocyclic receptors