In Vitro Efficacy Testing Services for Amyloidosis

We provide robust and sensitive in vitro screening and characterization platforms for accelerating the discovery and screening of potential therapies for Amyloidosis. Our services specifically enable the assessment of compound efficacy, aggregation inhibition, and molecular interactions relevant to amyloid protein misfolding and deposition. Key targets include amyloidogenic proteins such as amyloid-beta, transthyretin, and light chains, as well as associated signaling pathways. We support the evaluation of pathological processes such as amyloid aggregation, fibril formation, and cytotoxicity induced by amyloid deposits.

Our in vitro testing portfolio encompasses a wide range of biochemical and biophysical assays tailored to the investigation of amyloid-related mechanisms. These methods allow precise quantification of target engagement, aggregation status, and functional outcomes, supporting comprehensive drug candidate profiling.

Biolayer interferometry assay: Measures real-time binding interactions between amyloid proteins and therapeutic candidates, providing kinetic data without the need for labeling.

Chemiluminescent assay: Detects amyloidogenic events or target engagement with high sensitivity using light emission from chemical reactions.

ELISA assay: Quantifies protein levels or aggregation states via antibody-based detection, suitable for high-throughput screening.

Fluorescence resonance energy transfer (FRET) assay: Monitors proximity changes between labeled molecules, enabling detection of protein aggregation or inhibitor activity.

Fluorescent assay: Utilizes fluorescent dyes or probes to assess amyloid formation, aggregation kinetics, or compound efficacy.

Fluorescent polarization assay: Measures binding interactions and changes in molecular rotation, useful for studying amyloid-ligand interactions.

Homogeneous Time Resolved Fluorescence (HTRF) assay: Provides sensitive, low-background detection of amyloid targets or aggregates through energy transfer techniques.

Isothermal titration calorimetric assay: Quantifies the thermodynamics of binding events between amyloid proteins and test compounds.

Luciferine/luciferase assay: Employs bioluminescence to monitor cellular events or toxicity associated with amyloid pathology.

RNA assay: Detects changes in gene expression or RNA processing related to amyloidogenic pathways.

Radioactivity assay: Measures incorporation or displacement of radioactive labels to study binding, aggregation, or metabolic processing.

Surface plasmon resonance assay: Offers real-time, label-free analysis of molecular interactions, providing binding kinetics and affinity data for amyloid studies.

We quantify a suite of key pharmacological parameters to characterize compound potency, binding affinity, and efficacy in amyloid-related assays. These measurements are essential for ranking candidate molecules, optimizing lead selection, and supporting translational research.

EC-50: The effective concentration of a compound that produces 50% of its maximal effect, indicating functional potency.

IC-50: The concentration of an inhibitor required to reduce a specific biological or biochemical function by 50%, used for assessing inhibitory strength.

Kd: The equilibrium dissociation constant, reflecting the binding affinity between a ligand and its target; lower values indicate stronger binding.

Ki: The inhibition constant, representing the binding affinity of an inhibitor for its target, critical for evaluating competitive inhibitors.

MEC: The minimum effective concentration at which a compound shows a measurable pharmacological effect, important for dose optimization.

Recommended In Vitro Efficacy Tests

Amyloid Beta Precursor Protein

Amyloid Beta Precursor Protein (APP) is central to amyloidosis pathology as its cleavage produces amyloid-beta peptides, forming toxic aggregates. Testing APP is crucial for drug development targeting amyloid formation. Using biolayer interferometry and ELISA assays, our service measures key parameters including IC-50 (compound potency) and Kd (binding affinity), enabling precise evaluation of candidate drugs’ effects on APP processing and aggregation.

Caspase 3

Caspase 3 is a key executor of apoptosis, often activated in amyloidosis-related cell death. Caspase 3 testing is crucial for evaluating the apoptotic effects of candidate drugs in amyloidosis drug development. Our service employs a chemiluminescent assay to sensitively measure Caspase 3 activity, providing reliable quantification of Minimal Effective Concentration (MEC) for drug efficacy assessment. This supports informed decision-making in therapeutic screening.

Cereblon

Cereblon is a key E3 ligase modulator involved in the mechanism of action of several amyloidosis therapeutics. Accurate Cereblon testing is crucial for optimizing drug efficacy and safety in amyloidosis drug development. Using advanced techniques—including fluorescent polarization, chemiluminescence, HTRF, and FRET assays—this service measures essential parameters such as EC-50, IC-50, and Kd to assess compound potency, binding affinity, and inhibitory activity.

Nuclear Receptor Subfamily 3 Group C Member 1

Nuclear Receptor Subfamily 3 Group C Member 1 (NR3C1) is implicated in the regulation of inflammatory pathways relevant to Amyloidosis. Our testing service evaluates drug candidates by assessing NR3C1 modulation using luciferin/luciferase, chemiluminescent, RNA, and radioactivity assays. Key pharmacological parameters measured include EC-50, MEC, and Ki, enabling precise characterization of compound potency and efficacy—critical for advancing Amyloidosis drug development.

Transthyretin

Transthyretin (TTR) misfolding leads to amyloid deposits in amyloidosis. TTR testing is vital in drug development to identify compounds that inhibit TTR aggregation. Our service utilizes surface plasmon resonance, isothermal titration calorimetry, and fluorescent assays to assess compound binding and stabilization. Key parameters measured include IC₅₀ (compound potency) and Kd (binding affinity), providing essential data for advancing effective amyloidosis therapeutics.