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      Direct Observation of Amyloid β Behavior at Phospholipid Membrane Constructed on Gold Nanoparticles

      research-article
      Author(s): , , ,
      Publication date (Electronic):
      Journal: International Journal of Analytical Chemistry
      Publisher: Hindawi

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          Abstract

          Amyloid β (A β) is a potential biomarker of Alzheimer's disease (AD), and its fibrillation behavior is of interest and value. In this study, the A β behaviors on phospholipid membranes were observed by Membrane Surface-Enhanced Raman Spectroscopy (MSERS) method. Phospholipid (PL) membranes, consisting of DMPC and DMPS with a molar ratio of 9:1, were fabricated on gold nanoparticles with diameter of 100 nm (Au@PL). Enhancement of the Raman intensity of Au@PL was increased by A β, with enhancement factor about 40. The H-bonding network was disturbed in presence of NaCl which covered Au@PL and made Au@PL away from one another. When A β was applied with Au@PL, the H-bonding network was disturbed just after mixing. As the reaction reaches to equilibrium, A β attracted neighbouring Au@PL and induced aggregation of Au@PL which blocked the aggregation prone site of A β to inhibit further fibrillation. Based on our method, the A β behaviors at lipid membrane surface can be directly observed via enhanced Raman signals.

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          Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism.

          L. Nielsen, R. Khurana, A Coats … (2001)
          In the search for the molecular mechanism of insulin fibrillation, the kinetics of insulin fibril formation were studied under different conditions using the fluorescent dye thioflavin T (ThT). The effect of insulin concentration, agitation, pH, ionic strength, anions, seeding, and addition of 1-anilinonaphthalene-8-sulfonic acid (ANS), urea, TMAO, sucrose, and ThT on the kinetics of fibrillation was investigated. The kinetics of the fibrillation process could be described by the lag time for formation of stable nuclei (nucleation) and the apparent rate constant for the growth of fibrils (elongation). The addition of seeds eliminated the lag phase. An increase in insulin concentration resulted in shorter lag times and faster growth of fibrils. Shorter lag times and faster growth of fibrils were seen at acidic pH versus neutral pH, whereas an increase in ionic strength resulted in shorter lag times and slower growth of fibrils. There was no clear correlation between the rate of fibril elongation and ionic strength. Agitation during fibril formation attenuated the effects of insulin concentration and ionic strength on both lag times and fibril growth. The addition of ANS increased the lag time and decreased the apparent growth rate for insulin fibril formation. The ANS-induced inhibition appears to reflect the formation of amorphous aggregates. The denaturant, urea, decreased the lag time, whereas the stabilizers, trimethylamine N-oxide dihydrate (TMAO) and sucrose, increased the lag times. The results indicated that both nucleation and fibril growth were controlled by hydrophobic and electrostatic interactions. A kinetic model, involving the association of monomeric partially folded intermediates, whose concentration is stimulated by the air-water interface, leading to formation of the critical nucleus and thence fibrils, is proposed.
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            Inhibition of amyloid beta protein fibrillation by polymeric nanoparticles.

            Celia Cabaleiro-Lago, Fiona Quinlan-Pluck, Iseult Lynch … (2008)
            Copolymeric NiPAM:BAM nanoparticles of varying hydrophobicity were found to retard fibrillation of the Alzheimer's disease-associated amyloid beta protein (Abeta). We found that these nanoparticles affect mainly the nucleation step of Abeta fibrillation. The elongation step is largely unaffected by the particles, and once the Abeta is nucleated, the fibrillation process occurs with the same rate as in the absence of nanoparticles. The extension of the lag phase for fibrillation of Abeta is strongly dependent on both the amount and surface character of the nanoparticles. Surface plasmon resonance studies show that Abeta binds to the nanoparticles and provide rate and equilibrium constants for the interaction. Numerical analysis of the kinetic data for fibrillation suggests that binding of monomeric Abeta and prefibrillar oligomers to the nanoparticles prevents fibrillation. Moreover, we find that fibrillation of Abeta initiated in the absence of nanoparticles can be reversed by addition of nanoparticles up to a particular time point before mature fibrils appear.
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              Extracellular phosphorylation of the amyloid β-peptide promotes formation of toxic aggregates during the pathogenesis of Alzheimer's disease.

              Sathish Kumar, Nasrollah Rezaei-Ghaleh, Dick Terwel … (2011)
              Alzheimer's disease (AD) is the most common form of dementia and associated with progressive deposition of amyloid β-peptides (Aβ) in the brain. Aβ derives by sequential proteolytic processing of the amyloid precursor protein by β- and γ-secretases. Rare mutations that lead to amino-acid substitutions within or close to the Aβ domain promote the formation of neurotoxic Aβ assemblies and can cause early-onset AD. However, mechanisms that increase the aggregation of wild-type Aβ and cause the much more common sporadic forms of AD are largely unknown. Here, we show that extracellular Aβ undergoes phosphorylation by protein kinases at the cell surface and in cerebrospinal fluid of the human brain. Phosphorylation of serine residue 8 promotes formation of oligomeric Aβ assemblies that represent nuclei for fibrillization. Phosphorylated Aβ was detected in the brains of transgenic mice and human AD brains and showed increased toxicity in Drosophila models as compared with non-phosphorylated Aβ. Phosphorylation of Aβ could represent an important molecular mechanism in the pathogenesis of the most common sporadic form of AD.
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                Author and article information

                Contributors
                Keishi Suga:
                ORCID: http://orcid.org/0000-0001-8015-8729
                Hiroshi Umakoshi:
                ORCID: http://orcid.org/0000-0002-9241-853X
                Journal
                Journal ID (nlm-ta): Int J Anal Chem
                Journal ID (iso-abbrev): Int J Anal Chem
                Journal ID (publisher-id): IJAC
                Title: International Journal of Analytical Chemistry
                Publisher: Hindawi
                ISSN (Print): 1687-8760
                ISSN (Electronic): 1687-8779
                Publication date Collection: 2018
                Publication date (Electronic): 2 December 2018
                Volume: 2018
                Electronic Location Identifier: 2571808
                Affiliations
                Division of Chemical Engineering, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama-cho, Toyonaka, Osaka 560-8531, Japan
                Author notes

                Academic Editor: David M. Lubman

                Author information
                http://orcid.org/0000-0001-8015-8729
                http://orcid.org/0000-0002-9241-853X
                Article
                DOI: 10.1155/2018/2571808
                PMC ID: 6304496
                SO-VID: 8efb391f-d8df-4b63-ad88-9fb16da2bdd4
                Copyright © Copyright © 2018 Keishi Suga et al.
                License:

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 31 August 2018
                Date accepted : 11 November 2018
                Funding
                Funded by: Japan Society for the Promotion of Science
                Award ID: 26249116
                Award ID: 16K18279
                Funded by: Challenging Exploratory Research
                Award ID: T15K142040
                Categories
                Subject: Research Article

                ScienceOpen disciplines: Analytical chemistry
                Data availability:
                ScienceOpen disciplines: Analytical chemistry

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