Interaction between human amphipathic apolipoproteins and amyloid β-peptide: surface plasmon resonance studies

FEBS Letters ◽  
1996 ◽  
Vol 383 (1-2) ◽  
pp. 9-12 ◽  
Author(s):  
Vladimir V. Shuvaev ◽  
Gérard Siest
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Amyloid Β ◽  
Amyloid Β Peptide

scholarly journals Surface Plasmon Resonance Binding Kinetics of Alzheimer’s Disease Amyloid β Peptide-Capturing and Plaque-Binding Monoclonal Antibodies

Biochemistry ◽  
2009 ◽  
Vol 48 (43) ◽  
pp. 10405-10415 ◽  
Author(s):  
Muthu Ramakrishnan ◽  
Karunya K. Kandimalla ◽  
Thomas M. Wengenack ◽  
Kyle G. Howell ◽  
Joseph F. Poduslo
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Monoclonal Antibodies ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Amyloid Β ◽  
Binding Kinetics ◽  
Amyloid Β Peptide ◽  
Kinetics Of

scholarly journals Surface Plasmon Resonance Based Biosensors for Exploring the Influence of Alkaloids on Aggregation of Amyloid-β Peptide

Sensors ◽  
2011 ◽  
Vol 11 (4) ◽  
pp. 4030-4042 ◽  
Author(s):  
Bartłomiej Emil Kraziński ◽  
Jerzy Radecki ◽  
Hanna Radecka
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Amyloid Β ◽  
Amyloid Β Peptide

Surface Plasmon Resonance Imaging of Amyloid-β Aggregation Kinetics in the Presence of Epigallocatechin Gallate and Metals

2013 ◽  
Vol 85 (4) ◽  
pp. 2049-2055 ◽  
Author(s):  
Xin R. Cheng ◽  
Ben Y. H. Hau ◽  
Anthony J. Veloso ◽  
Sanela Martic ◽  
Heinz-Bernhard Kraatz ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Epigallocatechin Gallate ◽  
Amyloid Β ◽  
Aggregation Kinetics ◽  
Surface Plasmon Resonance Imaging ◽  
Resonance Imaging

scholarly journals Morphological analysis of Apolipoprotein E binding to Aβ Amyloid using a combination of Surface Plasmon Resonance, Immunogold Labeling and Scanning Electron Microscopy

2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Tohidul Islam ◽  
Anna L. Gharibyan ◽  
Cheng Choo Lee ◽  
Anders Olofsson
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Surface Plasmon Resonance ◽  
Apolipoprotein E ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Amyloid Β ◽  
Immunogold Labeling ◽  
Aβ Amyloid ◽  
Scanning Electron

Abstract Background Immunogold labeling in combination with transmission electron microscopy analysis is a technique frequently used to correlate high-resolution morphology studies with detailed information regarding localization of specific antigens. Although powerful, the methodology has limitations and it is frequently difficult to acquire a stringent system where unspecific low-affinity interactions are removed prior to analysis. Results We here describe a combinatorial strategy where surface plasmon resonance and immunogold labeling are used followed by a direct analysis of the sensor-chip surface by scanning electron microscopy. Using this approach, we have probed the interaction between amyloid-β fibrils, associated to Alzheimer’s disease, and apolipoprotein E, a well-known ligand frequently found co-deposited to the fibrillar form of Aβ in vivo. The results display a lateral binding of ApoE along the amyloid fibrils and illustrates how the gold-beads represent a good reporter of the binding. Conclusions This approach exposes a technique with generic features which enables both a quantitative and a morphological evaluation of a ligand-receptor based system. The methodology mediates an advantage compared to traditional immunogold labeling since all washing steps can be monitored and where a high stringency can be maintained throughout the experiment.

Surface plasmon resonance biosensor for the detection of tau-amyloid β complex

2020 ◽  
Vol 316 ◽  
pp. 128146
Author(s):  
Tomáš Špringer ◽  
Erika Hemmerová ◽  
Giusy Finocchiaro ◽  
Zdenka Krištofiková ◽  
Martin Vyhnálek ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Amyloid Β ◽  
Surface Plasmon Resonance Biosensor

Comparison of sensitivity of the refractometric methods of frustrated total internal reflection and surface plasmon resonance

2020 ◽  
pp. 44-49
Author(s):  
I. N. Pavlov
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Total Internal Reflection ◽  
Resonance Method ◽  
Internal Reflection ◽  
Optical Methods ◽  
Thin Boundary Layer ◽  
Experimental Conditions ◽  
Frustrated Total Internal Reflection

Two optical methods, namely surface plasmon resonance imaging and frustrated total internal reflection, are described in the paper in terms of comparing their sensitivity to change of refractive index of a thin boundary layer of an investigated medium. It is shown that, despite the fact that the theoretically calculated sensitivity is higher for the frustrated total internal reflection method, and the fact that usually in practice the surface plasmon resonance method, on the contrary, is considered more sensitive, under the same experimental conditions both methods show a similar result.

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