Creative Biolabs

Amyloid-beta 42 Inhibitor Screening Assay

One of the main pathological features of Alzheimer's disease is the fibrosis of Aβ42 and the deposition of amyloid plaques. The development and screening of Aβ42 inhibitors are often one of the main directions of AD drug development. With in-depth research on AD pathology and molecular biology, Creative Biolabs currently provides comprehensive and reliable screening services for Aβ42 inhibitors to customers all over the world.

Fibrosis of Aβ42

Amyloid plaque deposition caused by fibrosis of Aβ40 and Aβ42 tends to be the main pathological feature of AD, while Aβ42 is more hydrophobic and more prone to fibrosis than Aβ40, therefore, it is widely used to study the role of protein aggregation in the development of AD pathology and the screening or development of AD-targeted drug-like molecules. The aggregation of Aβ42 is a complex process. Aβ42 protein will first form low-molecular oligomers and then assemble into larger sheet-rich oligomers, resulting in higher-order aggregations with uneven size and shape. Finally, higher-order intermediates gradually disappear with the formation of fibers. Aβ42 deposition and intermediates may enhance oxidative stress and inflammation and lead to cellular damage.

Analysis of Aβ42 aggregation kinetics.Fig 1. Analysis of Aβ42 aggregation kinetics. (Bartolini, 2011)

Aβ42 Inhibitor Screening

The analysis of drug-like molecules that inhibit Aβ42 aggregation has been well studied, these compounds/chemicals include short antibody peptides, curcumin, hydroxyphenylalanine and its derivatives, asiaticol, myricetin, Caffeic acid, catechin, 8-hydroxyquinoline, etc. With the analysis and screening of such substances, assays based on cell or animal models have also been developed. Backed by our strong technical platform and theoretical knowledge, Creative Biolabs offers screening and identifying services to putative Aβ42-inhibiting compounds through drug-like molecular libraries, performing high-throughput screening experiments in yeast, PC12, or other cells to validate and confirm the anti-oligomerization activity of selected compounds. A series of pathological tissue sections and animal models are also at your disposal.

Screening of Aβ42 inhibitors using yeast.Fig 2. Screening of Aβ42 inhibitors using yeast. (Park, 2011)

We also screen compounds that inhibit the aggregation of Aβ42 by thioflavin T fluorescence assay, determined the cytotoxicity of Aβ42 by cytotoxicity assay and ROS detection, and determined the effect of the tested compounds on Aβ42 aggregation. In addition, we can also combine atomic force microscopy and mass spectrometry to directly characterize the morphology and size of Aβ42 aggregates. We are willing to improve our existing experimental protocols or tailor new experimental methods for you according to your needs and suggestions.

Effects of different compounds on the morphology of Aβ42 aggregates.Fig 3. Effects of different compounds on the morphology of Aβ42 aggregates. (Ma, 2021)

Our Service

Creative Biolabs is committed to the development and application of cutting-edge and reliable technology, through various microscopy techniques, high-throughput screening techniques, light scattering, fluorescence, colorimetry, chromatography and mass spectrometry to build a multi-method research platform and customize a reliable and highly reproducible experimental protocol for our customers. What we can do is not only identify and screen the Aβ42 inhibitory compounds you are interested in, but also help you study and explore the inhibitory mechanism and biochemical reaction of Aβ42 in detail according to your needs. Please do not hesitate to contact us for more information.


  1. Bartolini, M.; et al. Kinetic characterization of amyloid-beta 1-42 aggregation with a multimethodological approach. Analytical Biochemistry. 2011, 414: 215-225.
  2. Park, S.; et al. Understanding the complex phage-host interactions in biofilm communities. Annual Review of Virology. 2021, 8: 73-94.
  3. Ma, L.; et al. Development and validation of a yeast high-throughput screen for inhibitors of Aβ42 oligomerization. Disease Models and Mechanisms. 2011, 4: 822-831.
For Research Use Only. Not For Clinical Use.
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