Binding of the Alzheimer amyloid β-peptide to neuronal cell membranes by fluorescence correlation spectroscopy

Hossain, Shakil; Grande, Mirtha; Ahmadkhanov, Galib; Pramanik, Aladdin

doi:10.1016/j.yexmp.2007.01.008

Cited by 17 publications

(16 citation statements)

References 37 publications

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“…Although further work is clearly needed to define the aggregation process, the results from the pbICS analysis are consistent with and complimentary to other analyses using very different biophysical (FRET (31), FCS (32,33), and biochemical approaches (mass spectrometry ( (34)). In the cited FCS studies, it was concluded that the Ab peptide was predominantly monomeric and/or in small oligomers in the extracellular medium, but decreased in lateral movement due to cell-membrane binding and further oligomerization.…”

Section: Ab Peptide Aggregation By Pbicssupporting

confidence: 74%

Aggregation Distributions on Cells Determined by Photobleaching Image Correlation Spectroscopy

Ciccotosto

Kozer

Chow

et al. 2013

Biophysical Journal

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The organization of molecules into macromolecular (nanometer scale), supramolecular complexes (submicron-to-micron scale), and within subcellular domains, is an important architectural principle of cellular biology and biochemistry. Determining the precise nature and distribution of complexes within the cellular milieu is a challenging biophysical problem. Time-series analysis of laser scanning confocal microscopy images by image correlation spectroscopy (ICS) or fluctuation moments methods provides information on aggregation, flow, and dynamics of fluorescently tagged macromolecules. All the methods to date require a brightness standard to relate the experimental data to absolute aggregation. In this article, we show that ICS as a function of gradual photobleaching is a sensitive indicator of aggregation distribution on the submicron scale. Specifically, in photobleaching ICS, the extent of nonlinearity of the apparent cluster density as a function of bleaching is related to the size of clusters. The analysis is tested using computer simulations on model aggregate systems and then applied to an experimental determination of Aβ peptide aggregation on nerve cells. The analysis reveals time-dependent increases in Aβ1-42 peptide aggregation. Globally, the datasets could be described by a monomer-dimer-tetramer-hexamer or a monomer-dimer-trimer-pentamer model. The results demonstrate the utility of photobleaching with ICS for determining aggregation states on the supramolecular scale in intact cells without the requirement for a brightness standard.

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Section: Ab Peptide Aggregation By Pbicssupporting

confidence: 74%

Aggregation Distributions on Cells Determined by Photobleaching Image Correlation Spectroscopy

Ciccotosto

Kozer

Chow

et al. 2013

Biophysical Journal

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“…The N-termini of Aβ peptides are easily labeled with small, organic fluorophores including fluorescein, 926−930 rhodamine 928,930−932 and HiLyte 930,933,934 based dyes, and these N-terminal labels do not significantly perturb the peptides. 931,933,935,936 Because these peptides are extracellular, incubation of cells with fluorescently labeled peptides can provide valuable, physiologically relevant data on how Aβ peptides interact with the extracellular leaflet of plasma membranes.…”

Section: Theoretical and Experimental Methods To Study Idpsmentioning

confidence: 99%

“…939−941 At these concentrations in aqueous solution, fluorescent Aβ (1–40) and Aβ (1–42) peptides are mainly monomeric, with small populations of dimers and trimers. 860,934,942 Single molecule fluorescence photobleaching, 860,943 or multicolor 934 experiments, as well as fluorescence correlation methods 929,932 provide a way to monitor Aβ peptides-cell interactions at these physiologically relevant concentrations. In photobleaching experiments, both the fluorescence intensity and number of photobleaching steps were used to determine the number of labeled monomers in a single fluorescent spot.…”

Section: Theoretical and Experimental Methods To Study Idpsmentioning

confidence: 99%

Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)

Binolfi²,

et al. 2014

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“…Notably, the aggregation of polyglutamine in cells [24], a-synuclein aggregation [25] and its binding to vesicles [26] have been studied. In relation to Ab, FCS has been used to establish an in vitro saturation concentration of Ab [27], to test the interaction with aggregation inhibitors [28] and membranes [29,30], to study the depletion of oligomers under physiological conditions [23] and to determine the size distribution of Ab aggregates in solution [27,31,32]. Garai et al [27] used a maximum entropy fitting method (MEM-FCS), which allowed multiple aggregating species within the system to be analyzed.…”

Section: Introductionmentioning

confidence: 99%

Simultaneous measurement of a range of particle sizes during Aβ1–42 fibrillogenesis quantified using fluorescence correlation spectroscopy

Mittag¹,

Milani²,

Walsh

et al. 2014

Biochemical and Biophysical Research Communications

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a b s t r a c tLow molecular weight oligomers of amyloid beta (Ab) are important drivers of Alzheimer's disease. A decrease in Ab monomer levels in human cerebrospinal fluid (CSF) is observed in Alzheimers' patients and is a robust biomarker of the disease. It has been suggested that the decrease in monomer levels in CSF is due to the formation of Ab oligomers. A robust technique capable of identifying Ab oligomers in CSF is therefore desirable. We have used fluorescence correlation spectroscopy and a five Gaussian distribution model (5GDM) to monitor the aggregation of Ab 1-42 in sodium phosphate buffer and in artificial cerebrospinal fluid (ACSF). In buffer, several different sized components (monomer, oligomers, protofibrils and fibrils) can be identified simultaneously using 5GDM. In ACSF, the faster kinetics of fibrillogenesis leads to the formation of fibrils on very short timescales. This analysis method can also be used to monitor the aggregation of other proteins, nanoparticles or colloids, even in complex biological fluids.

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Binding of the Alzheimer amyloid β-peptide to neuronal cell membranes by fluorescence correlation spectroscopy

Cited by 17 publications

References 37 publications

Aggregation Distributions on Cells Determined by Photobleaching Image Correlation Spectroscopy

Aggregation Distributions on Cells Determined by Photobleaching Image Correlation Spectroscopy

Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)

Simultaneous measurement of a range of particle sizes during Aβ1–42 fibrillogenesis quantified using fluorescence correlation spectroscopy

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