Quantifying Amyloid β-Peptide (Aβ) Aggregation Using the Congo Red-Aβ (CR–Aβ) Spectrophotometric Assay

Klunk, William E.; Jacob, Robert F.; Mason, R. Preston

doi:10.1006/abio.1998.2933

Cited by 284 publications

(269 citation statements)

References 28 publications

Supporting

Mentioning

259

Contrasting

Order By: Relevance

“…Previous studies found that other mechanical disturbances, such as sonication 18 and agitation, 19 enhanced the fibril formation of different proteins, but during these studies, the difference between pulsed and continuous treatment was not studied. Although sonication is a common method to break up macromolecules, it can also be used to induce nucleation (i.e., an often used method in the sugar industry to control the size of the sugar crystals or to nucleate protein crystallization 25 ).…”

Section: Discussionmentioning

confidence: 96%

See 1 more Smart Citation

Shear Pulses Nucleate Fibril Aggregation

et al. 2006

View full text Add to dashboard Cite

We have studied the effect of shear flow on the formation of amyloid fibrils of the whey protein blactoglobulin. b-Lactoglobulin aggregates into long, thin, and semiflexible fibrils upon heating at low pH and low ionic strength. Solutions with a protein concentration of 0.5% (w/w) were used, and the formation of fibrils was quantified with flow-induced birefringence, a proportional measure of the length concentration of the fibrils. From the decay of the birefringence after cessation of the flow, a length distribution could be fitted. Pulsed and continuous shear treatment of the samples resulted in a comparable enhancement of the fibrillar growth as compared to the fibrillar growth under quiescent conditions. This indicates that the onset of shear flow is the key parameter for the enhancement of fibrillar growth and not the continuous shear flow itself. This behavior is comparable to a nucleation-like process, during which preaggregates of the fibrils are induced during the onset of the flow and orthokinetic coagulation is absent. However, a difference was present in the length distribution between the pulsed and continuously sheared samples, which can be explained by the homogenizing effect of shear flow.

show abstract

Section: Discussionmentioning

confidence: 96%

“…Other methods that can be used to measure the fibril concentration include the binding of fluorescent dyes (e.g., Congo Red 19,20 and thioflavin T 16,17 ), but these methods give no information on the fibril length distribution. During this study, flow-induced birefringence was used to analyze the fibril solution.…”

Section: Introductionmentioning

confidence: 99%

Shear Pulses Nucleate Fibril Aggregation

et al. 2006

View full text Add to dashboard Cite

show abstract

“…Its absorption spectrum shifts from orange-red to rose-red when it binds to fibrillar Ab1-40. CR binds to amyloid only in the b-pleated sheet conformation (Ashburn et al, 1996;Klunk et al, 1999). Because it has a high affinity for amyloid in brain slices, it is used as a targeting head group which can increase the ability of the complex to bind amyloid plaques in CR-BSA-(Gd-DTPA)n. The ability of CR-BSA-(Gd-DTPA)n to bind Ab protein was demonstrated by the histochemistry staining of APP/PS1 mouse brain sections.…”

Section: Discussionmentioning

confidence: 99%

Detection of Aβ Plaques by a Novel Specific MRI Probe Precursor CR‐BSA‐(Gd‐DTPA)n in APP/PS1 Transgenic Mice

Cui

et al. 2010

The Anatomical Record

View full text Add to dashboard Cite

Amyloid plaques are one of the hallmarks of Alzheimer's disease (AD). The lack of specific probes that can detect individual senile plaques in AD has prompted the development of magnetic resonance imaging (MRI) probes. In this study, based on DTPA-gadolinium (III) and congo red (CR), a novel specific MRI probe precursor CR-BSA-(Gd-DTPA)n was successfully synthesized. Its ability to bind to amyloid plaques was evaluated by brain sections from APP/PS1 transgenic mice. Its specificity for Ab plaques was further demonstrated by immunohistochemistry (IHC) staining with the monoclonal antibody to the Ab protein. Meanwhile, the amyloid deposits detected by the CR-BSA-(Gd-DTPA)n were matched to the amyloid deposits detected by Ab specific antibody. We also found that a few amyloid-like deposits which was not detected by IHC. The findings indicated that the probe perhaps could detect the neurofibrillary tangles (NFT) similar to the effect of CR itself, and this will be verified in future experiments. The works suggested that the Ab protein-specific magnetic resonance contrast agent precursor CR-BSA-(Gd-DTPA)n can be used as a potential fluorescence and MR multi-modal imaging probe precursor to display individual senile plaques in AD. Anat Rec, 293:2136Rec, 293: -2143

show abstract

“…Congo Red Binding-CR binding was detected spectrophotometrically according to the method of Klunk et al (39). Briefly, CR (1:5, mol of protein:mol of CR) was added to the protein samples, and the absorbance spectrum (425-650 nm) of the mixture was collected on a Shimadzu UV-1800 spectrophotometer.…”

mentioning

confidence: 99%

Myeloperoxidase-mediated Methionine Oxidation Promotes an Amyloidogenic Outcome for Apolipoprotein A-I

Chan¹,

Witkowski²,

Gantz

et al. 2015

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Amyloids made of apolipoprotein A-I (apoA-I) contribute to the growth of the atherosclerotic plaques. Results: ApoA-I methionine oxidation by physiological levels of myeloperoxidase induces amyloid formation. Conclusion: Myeloperoxidase-mediated oxidation not only impairs the physiological functions of apoA-I but also promotes protein loss in form of amyloids. Significance: Our findings identify the physiological mechanism transforming wild-type apoA-I into an amyloidogenic protein.

show abstract

Quantifying Amyloid β-Peptide (Aβ) Aggregation Using the Congo Red-Aβ (CR–Aβ) Spectrophotometric Assay

Cited by 284 publications

References 28 publications

Shear Pulses Nucleate Fibril Aggregation

Shear Pulses Nucleate Fibril Aggregation

Detection of Aβ Plaques by a Novel Specific MRI Probe Precursor CR‐BSA‐(Gd‐DTPA)n in APP/PS1 Transgenic Mice

Myeloperoxidase-mediated Methionine Oxidation Promotes an Amyloidogenic Outcome for Apolipoprotein A-I

Contact Info

Product

Resources

About