scholarly journals Multi-spectroscopic monitoring of molecular interactions between an amino acid-functionalized ionic liquid and potential anti-Alzheimer's drugs

RSC Advances ◽  
2020 ◽  
Vol 10 (64) ◽  
pp. 38873-38883
Author(s):  
Srishti Sharma ◽  
Manoj Kumar Banjare ◽  
Namrata Singh ◽  
Jan Korábečný ◽  
Kamil Kuča ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Ionic Liquid ◽  
Ionic Liquids ◽  
Amino Acid ◽  
Molecular Interactions ◽  
Amyloid Fibrils ◽  
Functionalized Ionic Liquid ◽  
Inhibition Effect ◽  
Spectroscopic Monitoring

Ionic liquids mediated interactions are an expedient approach that exhibit inhibition effect on amyloid fibrils which is beneficial for the treatment of Alzheimer's disease.

Liquid crystalline ordering of paired helical filaments in neurofibrillary tangles of Alzheimer's disease

1986 ◽  
Vol 44 ◽  
pp. 348-349
Author(s):  
D.F. Clapin ◽  
V.J.A. Montpetit
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Neurofibrillary Tangles ◽  
Liquid Crystalline ◽  
Amyloid Fibrils ◽  
Geometric Analysis ◽  
Paired Helical Filaments ◽  
Microscopic Level ◽  
Light Microscopic Level ◽  
Regular Spacing

Alzheimer's disease is characterized by the accumulation of abnormal filamentous proteins. The most important of these are amyloid fibrils and paired helical filaments (PHF). PHF are located intraneuronally forming bundles called neurofibrillary tangles. The designation of these structures as "tangles" is appropriate at the light microscopic level. However, localized domains within individual tangles appear to demonstrate a regular spacing which may indicate a liquid crystalline phase. The purpose of this paper is to present a statistical geometric analysis of PHF packing.

Heterogenization of amine-functionalized ionic liquids using graphene oxide as a support material: a highly efficient catalyst for the synthesis of 3-substituted indoles via Yonemitsu-type reaction

2017 ◽  
Vol 41 (24) ◽  
pp. 15545-15554 ◽  
Author(s):  
Charu Garkoti ◽  
Javaid Shabir ◽  
Padmini Gupta ◽  
Manisha Sharma ◽  
Subho Mozumdar
Keyword(s):  
Ionic Liquid ◽  
Graphene Oxide ◽  
Ionic Liquids ◽  
Recyclable Catalyst ◽  
Support Material ◽  
Efficient Catalyst ◽  
Functionalized Ionic Liquid ◽  
Type Reaction ◽  
Highly Efficient ◽  
Amine Functionalized

Heterogenization of amine functionalized ionic liquid and its application as an efficient and recyclable catalyst.

Computational analysis of the effect of [Tea][Ms] and [Tea][H2PO4] ionic liquids on the structure and stability of Aβ(17–42) amyloid fibrils

2021 ◽  
Vol 23 (11) ◽  
pp. 6695-6709
Author(s):  
D. Gobbo ◽  
A. Cavalli ◽  
P. Ballone ◽  
A. Benedetto
Keyword(s):  
Ionic Liquid ◽  
Hydrogen Bonding ◽  
Ionic Liquids ◽  
Liquid Water ◽  
Computational Analysis ◽  
Amyloid Fibrils ◽  
Aβ Peptides ◽  
Structure And Stability ◽  
Water Solutions ◽  
Kinetics Of

Tight coordination of peptides by organic anions driven by hydrogen bonding affects the fibrillation kinetics of Aβ peptides in ionic liquid/water solutions.

scholarly journals Formation of Toxic Amyloid Fibrils by Amyloidβ-Protein on Ganglioside Clusters

2011 ◽  
Vol 2011 ◽  
pp. 1-7 ◽  
Author(s):  
Katsumi Matsuzaki
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Physicochemical Properties ◽  
Lipid Rafts ◽  
Molecular Mechanisms ◽  
Amyloid Fibrils ◽  
Protein A ◽  
Pivotal Role ◽  
Membrane Interaction

It is widely accepted that the conversion of the soluble, nontoxic amyloidβ-protein (Aβ) monomer to aggregated toxic Aβrich inβ-sheet structures is central to the development of Alzheimer’s disease. However, the mechanism of the abnormal aggregation of Aβin vivo is not well understood. Accumulating evidence suggests that lipid rafts (microdomains) in membranes mainly composed of sphingolipids (gangliosides and sphingomyelin) and cholesterol play a pivotal role in this process. This paper summarizes the molecular mechanisms by which Aβaggregates on membranes containing ganglioside clusters, forming amyloid fibrils. Notably, the toxicity and physicochemical properties of the fibrils are different from those of Aβamyloids formed in solution. Furthermore, differences between Aβ-(1–40) and Aβ-(1–42) in membrane interaction and amyloidogenesis are also emphasized.

scholarly journals Modeling the β secretase cleavage site and humanizing Amyloid-Beta Precursor Protein in rat and mouse to study Alzheimer Disease.

2020 ◽  
Author(s):  
Lutgarde Serneels ◽  
Dries T'Syen ◽  
Laura Perez-Benito ◽  
Tom Theys ◽  
Bart De Strooper
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amino Acid ◽  
Alzheimer Disease ◽  
Early Onset ◽  
Computational Modelling ◽  
Original Strain ◽  
Rodent Models ◽  
App Processing

Abstract Background Three amino acid differences between rodent and human APP affect medically important features including β-secretase cleavage of APP and aggregation of the Aβ peptide(1–3). Most rodent models for Alzheimer’s disease (AD) are therefore based on the human APP sequence expressed from artificial mini-genes randomly inserted in the rodent genome. While these models mimic rather well biochemical aspects of the disease such as Aβ-aggregation, they are also prone to overexpression artifacts and to complex phenotypical alterations due to genes affected in or close to the insertion sites of the mini-genes(4,5). Knock-in strategies introducing clinical mutants in a humanized endogenous rodent APP sequence(6) represent useful improvements, but need to be compared with appropriate humanized wild type (WT) mice.Methods Computational modelling of the human β-CTF bound to BACE1 was used to study the differential processing of rodent and human APP. We humanized the three pivotal residues G676R, F681Y and R684H (labeled according to the human APP770 isoform) in the mouse as well as in the rat by a CRISPR-Cas9 approach. These new models, termed mouse and rat App hu/hu , express APP from the endogenous promotor. We also introduced the early-onset familial Alzheimer’s disease (FAD) mutation M139T into the endogenous Rat Psen 1 gene.Results We show that the three amino acid substitutions in the rodent sequence lower the affinity of APP substrate for BACE1 cleavage. The effect on β-secretase processing was confirmed as both humanized rodent models produce three times more (human) Aβ compared to their WT rodent original strain. These models represent suitable controls or starting points for studying the effect of transgenes or knock-in mutations on APP processing(6). We introduced the early-onset familial Alzheimer disease (FAD) mutation M139T into the endogenous Rat Psen 1 gene and provide an initial characterization of Aβ processing in this novel rat AD model.Conclusion The different humanized APP models (rat and mouse) expressing human Aβ and PSEN1 M139T are valuable controls to study APP processing in vivo and allow to implement the use of human Aβ Elisa which is more sensitive than their rodent counterpart. These animals will be made available to the research community.

Sign in / Sign up

Export Citation Format

Share Document