Online citations, reference lists, and bibliographies.
← Back to Search

Biosensor‐based Label‐free Assays Of Amyloid Growth

D. A. White, A. Buell, C. Dobson, M. Welland, T. Knowles
Published 2009 · Chemistry, Medicine

Cite This
Download PDF
Analyze on Scholarcy
Share
Uncontrolled fibrous protein aggregation is implicated in a range of aberrant biological phenomena. Much effort has consequently been directed towards establishing quantitative in vitro assays of this process with the aim of probing amyloid growth in molecular detail as well as elucidating the effect of additional species on this reaction. In this paper, we discuss some recent approaches based on label‐free technologies focussed on achieving these objectives. Several biosensor techniques have been developed to monitor biomolecular assembly without the requirement for fluorophore marker molecules; in particular quartz crystal microbalance and surface plasmon resonance measurements provide advantageous alternatives to traditional spectroscopic methods and are currently receiving increasing attention in the context of amyloid growth assays.
This paper references
10.1073/pnas.0803086105
Direct characterization of amyloidogenic oligomers by single-molecule fluorescence
Angel Orte (2008)
10.1016/S0003-2670(01)95290-0
Frequency shifts of piezoelectric quartz crystals immersed in organic liquids
T. Nomura (1982)
Lipocalintype prostaglandin D synthase/beta-trace is a major amyloid beta-chaperone in human cerebrospinal fluid
T. Kanekiyo (2007)
10.1021/ja710310c
Modification of fluorophore photophysics through peptide-driven self-assembly.
Kevin J. Channon (2008)
10.1126/SCIENCE.1067484
Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation
M. Chapman (2002)
10.1021/LA950763D
Effect of Surface Film Structure on the Quartz Crystal Microbalance Response in Liquids
L. Daikhin (1996)
10.1146/ANNUREV.BIOCHEM.75.101304.123901
Protein misfolding, functional amyloid, and human disease.
F. Chiti (2006)
10.1074/jbc.271.15.8545
Arrest of -Amyloid Fibril Formation by a Pentapeptide Ligand (*)
L. Tjernberg (1996)
10.1016/j.bios.2008.03.036
Highly specific label-free protein detection from lysed cells using internally referenced microcantilever sensors.
Wenmiao Shu (2008)
Label-free detection of amyloid growth with microcantilever
T.P.J. Knowles (2008)
10.1021/AC0100897
Direct and quantitative detection of bacteriophage by "hearing" surface detachment using a quartz crystal microbalance.
F. Dultsev (2001)
10.1016/J.AB.2004.01.014
Kinetic analysis of beta-amyloid fibril elongation.
M. Cannon (2004)
Small heat shock protein HspB8: its distribution in Alzheimer's disease brains and its inhibition of amyloid-beta protein aggregation and cerebrovascular amyloid-beta toxicity.
M. M. Wilhelmus (2006)
10.1073/pnas.0701585104
Lipocalin-type prostaglandin D synthase/β-trace is a major amyloid β-chaperone in human cerebrospinal fluid
Takahisa Kanekiyo (2007)
10.1074/JBC.M011499200
Is Congo Red an Amyloid-specific Dye?*
R. Khurana (2001)
10.1021/BI049828E
Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p.
L. Bousset (2004)
10.1016/S0076-6879(99)09027-8
Analysis of fibril elongation using surface plasmon resonance biosensors.
D. Myszka (1999)
10.1149/1.1497173
Characterization of the Viscoelasticity and the Surface Roughness of Electrochemically Prepared Conducting Polymer Films by Impedance Measurements at Quartz Crystals
A. Bund (2002)
10.1016/S0076-6879(98)95044-3
Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors.
Myszka (1997)
10.1529/BIOPHYSJ.107.109686
Quartz crystal microbalance studies of multilayer glucagon fibrillation at the solid-liquid interface.
M. B. Hovgaard (2007)
10.1021/BI050700M
Binding of amyloidogenic transthyretin to the plasma membrane alters membrane fluidity and induces neurotoxicity.
Xu Hou (2005)
10.1016/S0925-4005(98)00321-9
Surface plasmon resonance sensors: review
J. Homola (1999)
10.1016/J.TIBS.2007.03.003
Functional amyloid--from bacteria to humans.
Douglas M. Fowler (2007)
10.1073/PNAS.90.8.3334
Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane.
S. Zhang (1993)
10.1046/j.1471-4159.2003.01552.x
Cholesterol is necessary both for the toxic effect of Aβ peptides on vascular smooth muscle cells and for Aβ binding to vascular smooth muscle cell membranes
S. Subasinghe (2003)
10.1021/BI020369W
Kinetic modeling and determination of reaction constants of Alzheimer's beta-amyloid fibril extension and dissociation using surface plasmon resonance.
K. Hasegawa (2002)
10.1021/LA00020A054
Influence of the surface morphology on the quartz crystal microbalance response in a fluid
M. Urbakh (1994)
10.1038/nature02264
Folding proteins in fatal ways
D. Selkoe (2003)
10.1021/AC00285A062
Frequency of a quartz microbalance in contact with liquid
K. Kanazawa (1985)
10.1126/SCIENCE.7909170
[URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae.
R. Wickner (1994)
10.1016/S0006-3495(98)74057-3
Surface specific kinetics of lipid vesicle adsorption measured with a quartz crystal microbalance.
C. A. Keller (1998)
Arrest of beta-Amyloid Fibril Formation by a Pentapeptide Ligand
J. N. slund (1996)
10.1038/nature02261
Protein folding and misfolding
C. Dobson (2003)
10.1039/A703137H
Simultaneous frequency and dissipation factor QCM measurements of biomolecular adsorption and cell adhesion.
M. Rodahl (1997)
10.1038/nature05741
Weighing of biomolecules, single cells and single nanoparticles in fluid
T. Burg (2007)
10.1038/nrg1616
Prions as adaptive conduits of memory and inheritance
J. Shorter (2005)
10.1074/jbc.M606856200
Hsp40 Interacts Directly with the Native State of the Yeast Prion Protein Ure2 and Inhibits Formation of Amyloid-like Fibrils*
Hui-Yong Lian (2007)
10.1126/SCIENCE.1087348
Games Played by Rogue Proteins in Prion Disorders and Alzheimer's Disease
A. Aguzzi (2003)
10.1073/PNAS.94.18.9773
The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog.
V. Coustou (1997)
10.1002/jmr.928
Survey of the year 2007 commercial optical biosensor literature
R. Rich (2008)
10.1238/Physica.Regular.059a00391
Viscoelastic Acoustic Response of Layered Polymer Films at Fluid-Solid Interfaces: Continuum Mechanics Approach
M. Voinova (1999)
10.1371/journal.pbio.0060017
Amyloid as a Depot for the Formulation of Long-Acting Drugs
S. Maji (2008)
10.1016/S0959-440X(99)00045-7
Implications of macromolecular crowding for protein assembly.
A. Minton (2000)
10.1021/JA065222X
Investigating the molecular mechanisms of in-plane mechanochemistry on cantilever arrays.
Moyu Watari (2007)
10.1073/pnas.0703793104
Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Aβ protofibrils
G. Habicht (2007)
10.1016/j.biomaterials.2007.11.028
Functionalised amyloid fibrils for roles in cell adhesion.
S. Gras (2008)
Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity.
M. M. Wilhelmus (2006)
Casting metal nanowires within discrete selfassembled peptide
M. Reches (2003)
10.1021/BI0156254
Affinity-Based Inhibition of β-Amyloid Toxicity†
C. Cairo (2002)
10.1038/35065632
Conformational diversity in a yeast prion dictates its seeding specificity
P. Chien (2001)
10.1016/J.COLSURFB.2007.03.014
Kinetics and enthalpy measurements of interaction between beta-amyloid and liposomes by surface plasmon resonance and isothermal titration microcalorimetry.
Ming-Shen Lin (2007)
10.1021/AC00068A033
Effect of surface roughness on the response of thickness-shear mode resonators in liquids
S. J. Martin (1993)
10.1006/JSBI.2000.4241
Self-assembly of beta-amyloid 42 is retarded by small molecular ligands at the stage of structural intermediates.
B. Bohrmann (2000)
10.1111/j.1747-0285.2006.00446.x
Convenient Method for Monitoring Aβ Aggregation by Quartz‐Crystal Microbalance
H. Okuno (2006)
10.1016/S0968-0004(99)01445-0
Protein misfolding, evolution and disease.
C. Dobson (1999)
10.1016/j.ab.2008.03.022
Quartz crystal microbalance analysis of growth kinetics for aggregation intermediates of the amyloid-beta protein.
J. A. Kotarek (2008)
10.1038/nchembio.131
Amyloid formation by globular proteins under native conditions.
F. Chiti (2009)
10.1073/pnas.0610659104
Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass
T. Knowles (2007)
10.1371/journal.pbio.0040006
Functional Amyloid Formation within Mammalian Tissue
Douglas M. Fowler (2006)
10.1088/0957-4484/19/38/384007
Label-free detection of amyloid growth with microcantilever sensors.
T. Knowles (2008)
10.1016/S0165-022X(03)00103-9
Kinetics of adsorption of β-amyloid peptide Aβ(1–40) to lipid bilayers
J. Kremer (2003)
10.1021/AC049859F
Micromechanical detection of proteins using aptamer-based receptor molecules.
C. Savran (2004)
10.1016/0168-9525(94)90029-9
URE 3 ] as an Altered URE 2 Protein : Evidence for a Prion Analog in Saccharomyces cerevisiae
D. Cheresh
10.1002/1521-3773(20001117)39:22<4004::AID-ANIE4004>3.0.CO;2-2
Piezoelectric Mass-Sensing Devices as Biosensors-An Alternative to Optical Biosensors?
Janshoff (2000)
10.1126/science.1151839
Amyloid Fibrils of the HET-s(218–289) Prion Form a β Solenoid with a Triangular Hydrophobic Core
C. Wasmer (2008)
10.1016/j.sbi.2007.12.005
Insights into the mechanism of prion propagation.
S. Perrett (2008)
10.1038/nbt874
Fabrication of novel biomaterials through molecular self-assembly
S. Zhang (2003)
10.1038/nbt0901-833
Direct and sensitive detection of a human virus by rupture event scanning
M. Cooper (2001)
10.1038/nnano.2006.134
Rapid and label-free nanomechanical detection of biomarker transcripts in human RNA
J. Zhang (2006)
Kinetics of adsorption of beta-amyloid peptide Abeta(1-40) to lipid bilayers.
J. Kremer (2003)
Amyloid fibrils of the HET-s(218–289) prion form a beta solenoid with a triangular hydrophobic
C. Wasmer (2008)
10.1073/pnas.0712197105
Transthyretin protects Alzheimer's mice from the behavioral and biochemical effects of Aβ toxicity
J. Buxbaum (2008)
10.1038/nnano.2006.139
Controlled patterning of aligned self-assembled peptide nanotubes
M. Reches (2006)
10.1111/j.1747-0285.2007.00509.x
Development of aggregation inhibitors for amyloid‐β peptides and their evaluation by quartz‐crystal microbalance
H. Okuno (2007)
10.1038/nrmicro1127
Amyloids — a functional coat for microorganisms
M. Gebbink (2005)
10.1126/SCIENCE.1082387
Casting Metal Nanowires Within Discrete Self-Assembled Peptide Nanotubes
Meital Reches (2003)
10.1038/nnano.2008.398
Quantitative time-resolved measurement of membrane protein-ligand interactions using microcantilever array sensors.
T. Braun (2009)
Affinity-based inhibition of beta-amyloid toxicity.
C. Cairo (2002)
10.1021/ac7019514
Surface plasmon resonance analysis of Alzheimer's beta-amyloid aggregation on a solid surface: from monomers to fully-grown fibrils.
Jungki Ryu (2008)
10.1007/bf01337937
Verwendung von Schwingquarzen zur Wägung dünner Schichten und zur Mikrowägung
G. Sauerbrey (1959)
10.1016/0022-1759(91)90331-9
Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system.
R. Karlsson (1991)
10.1016/J.JSB.2004.08.002
The binding of thioflavin-T to amyloid fibrils: localisation and implications.
M. Krebs (2005)
10.1021/jp805560c
Thioflavin T hydroxylation at basic pH and its effect on amyloid fibril detection.
V. Foderà (2008)
10.1016/S0003-2670(00)86049-3
Piezoelectric immuno sensor for the detection of candida albicans microbes
H. Muramatsu (1986)
10.1038/nature03679
Structural insights into a yeast prion illuminate nucleation and strain diversity
R. Krishnan (2005)
10.1002/JMR.753
Survey of the year 2004 commercial optical biosensor literature
R. Rich (2005)
10.1002/cbic.200900144
Position‐Dependent Electrostatic Protection against Protein Aggregation
A. Buell (2009)
10.1021/AC0107610
Influence of roughness on the admittance of the quartz crystal microbalance immersed in liquids.
L. Daikhin (2002)
10.1126/science.1150057
Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils
T. Knowles (2007)
10.1126/SCIENCE.288.5464.316
Translating biomolecular recognition into nanomechanics.
J. Fritz (2000)
10.5860/choice.38-2763
Mechanical Response of Polymers: An Introduction
A. Wineman (2000)
10.1016/j.cbpa.2008.02.011
Protein misfolding and disease: from the test tube to the organism.
Leila M. Luheshi (2008)
Folding proteins in fatal
D. J. Selkoe (2003)
10.1016/j.jmb.2008.01.057
Promotion of amyloid beta protein misfolding and fibrillogenesis by a lipid oxidation product.
L. Liu (2008)
10.1021/bi701522m
Formation of a high affinity lipid-binding intermediate during the early aggregation phase of alpha-synuclein.
D. Smith (2008)



This paper is referenced by
10.1016/j.ymeth.2010.11.009
Studying the effects of chaperones on amyloid fibril formation.
H. Zhang (2011)
10.1016/j.bbapap.2012.07.013
Kinetic intermediates of amyloid fibrillation studied by hydrogen exchange methods with nuclear magnetic resonance.
Y. Lee (2012)
10.1002/jbio.201100132
Fibrillogenesis of human β2 -microglobulin in three-dimensional silicon microstructures.
S. Merlo (2012)
High-Resolution Near-Field Optical Microscopy of Biological Molecules on Gold Surfaces
L. Hennemann (2011)
10.1039/c1cp22283j
Probing small molecule binding to amyloid fibrils.
A. Buell (2011)
10.1039/C4AY01237B
Low-fouling SPR detection of lysozyme and its aggregates
I. Mihai (2014)
10.1021/ja411577t
The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation.
Nikolai Lorenzen (2014)
10.1016/b978-0-444-53794-2.00009-4
Binding and Dissociation of Biomarkers for Alzheimer's Disease on Biosensor Surfaces
A. Sadana (2014)
10.1021/ac501343b
Characterizing α-helical peptide aggregation on supported lipid membranes using microcantilevers.
Jinghui Wang (2014)
Développement d’un système à ondes acoustiques pour le suivi rhéologique de la polymérisation de protéines. Application à la maladie d’Alzheimer.
P. Didier (2017)
10.1101/cshperspect.a010454
Protein solubility and protein homeostasis: a generic view of protein misfolding disorders.
M. Vendruscolo (2011)
10.1016/J.SNB.2012.04.064
DNA-based biosensor platforms for the detection of TP53 mutation
Zeynep Altintas (2012)
10.1002/PPSC.201400222
Structure-Making Effects of Metal Nanoparticles in Amyloid Peptide Fibrillation
A. Gladytz (2015)
10.2147/NDD.S39421
Nanobiosensors: the future for diagnosis of disease?
S. Prasad (2014)
10.1080/13102818.2014.901680
Novel insights into amylin aggregation
Karen Pillay (2014)
10.1002/smll.201303242
Amyloid-β aggregation with gold nanoparticles on brain lipid bilayer.
H. Lee (2014)
10.1039/c3lc51058a
Resolution enhancement of suspended microchannel resonators for weighing of biomolecular complexes in solution.
Mario M. Modena (2014)
10.1002/bit.27380
Label‐free, chronological and selective detection of aggregation and fibrillization of amyloid β protein in serum by microcantilever sensor immobilizing cholesterol‐incorporated liposome
T. Taniguchi (2020)
10.2174/1381612822666160518141911
AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species
F. S. Ruggeri (2016)
10.3233/JPD-130252
Can intrabodies serve as neuroprotective therapies for Parkinson's disease? Beginning thoughts.
M. A. Bhatt (2013)
10.1074/jbc.M110.208934
Relationship between Prion Propensity and the Rates of Individual Molecular Steps of Fibril Assembly*
Yi-Qian Wang (2011)
10.5075/epfl-thesis-6597
New Insights Into Amyloid Formation and Structure by Innovative Atomic Force Microscopy Methods
F. S. Ruggeri (2015)
10.1021/ja909997e
Protein aggregation in crowded environments.
D. A. White (2010)
10.3390/s110404030
Surface Plasmon Resonance Based Biosensors for Exploring the Influence of Alkaloids on Aggregation of Amyloid-β Peptide
B. E. Krazinski (2011)
10.1002/anie.201108040
Detailed analysis of the energy barriers for amyloid fibril growth.
A. Buell (2012)
Misfolding Disorders Protein Solubility and Protein Homeostasis : A Generic View of Protein
L. Stein (2011)
10.1007/978-1-60327-223-0_9
Probing protein aggregation with quartz crystal microbalances.
T. Knowles (2011)
10.1007/s00216-018-1142-3
Interactions between elastin-like peptides and an insulating poly(ortho-aminophenol) membrane investigated by AFM and XPS
M. E. Carbone (2018)
Detection of Alzheimer's disease biomarkers and mycotoxins using spectroscopic ellipsometry
M. K. Mustafa (2011)
10.1016/j.bios.2016.04.080
Versatile SPR aptasensor for detection of lysozyme dimer in oligomeric and aggregated mixtures.
A. Vasilescu (2016)
10.1063/1.4902131
Dry-mass sensing for microfluidics
T. Muller (2014)
10.1002/cbic.201000412
Amyloid Assemblies: Protein Legos at a Crossroads in Bottom‐Up Synthetic Biology
R. Giraldo (2010)
See more
Semantic Scholar Logo Some data provided by SemanticScholar