Enzyme Inhibition Screening
Enzyme Inhibition Screening - Related Videos
08:10
Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
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Cited by 7 •
2016
This work presents a method of high-throughput screening using a universal genetic enzyme screening system that can be theoretically applied to over 200 enzymes. Here, the single screening system identifies three different enzymes (lipase, cellulase, and alkaline phosphatase) by simply changing the substrate used (p-nitrophenyl acetate, p-nitrophenyl-β-D-cellobioside, and phenyl phosphate).
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Enzyme Inhibition
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2025
Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure. Competitive inhibitors occupy the active site of enzymes, making them unable to accommodate the substrate. However, sufficiently high...
03:49
Chromogenic Polymer Hydrogel-Based Enzyme Screening Assay: A High Throughput Method to Screen the Carbohydrate-Active Enzymes Using Synthetic Substrates
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2025
In this video, we demonstrate a high throughput assay for carbohydrate-active enzyme screening using insoluble chromogenic polymer hydrogel substrates. The enzyme degrades these substrates into a soluble colored product that can be quantified by measuring the color intensity of the product.
03:47
Microscopic Assessment of Enzyme-Mediated Inhibition of Biofilm Formation
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2026
Source: Tay, S. B., et.al. Anti-virulent Disruption of Pathogenic Biofilms using Engineered Quorum-quenching Lactonases. J. Vis. Exp. (2016)This video demonstrates the process of inhibiting biofilm formation by introducing an enzyme that disrupts bacterial cell signaling. The enzyme prevents the bacteria from producing extracellular polymeric substances, thereby reducing biofilm development on a glass-bottomed microdish. Finally, the biofilm structure is visualized using fluorescent lectins and...
08:11
Measuring Influenza Neuraminidase Inhibition Antibody Titers by Enzyme-linked Lectin Assay
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Cited by 54 •
2016
We describe the enzyme-linked lectin assay (ELLA) for measuring influenza neuraminidase (NA)-inhibition antibody titers in sera. The assay uses peanut agglutinin to quantify galactose residues that become accessible when NA removes sialic acid from fetuin-coated, 96-well plates.
FAQs
Classifying the observed inhibition pattern adds mechanistic meaning to a reduction in catalytic activity. It helps investigators move beyond asking whether a compound works and toward understanding how it may interact with the enzyme system. That distinction can clarify the inhibitor’s mechanism, support lead-compound evaluation, and guide which molecules merit further biochemical investigation.
Testing several inhibitor concentrations shows whether the activity change can be described across a concentration range rather than at one exposure. The resulting concentration-response data can support an IC50 estimate, which summarizes the concentration associated with a defined level of inhibition in the assay. This gives screening results a quantitative basis for comparing candidate compounds.
Testing a compound against related enzymes helps determine whether its inhibitory effect appears preferential or broadly distributed across the enzyme group. This selectivity assessment adds context that a single-enzyme result cannot provide. Compounds showing a more favorable activity pattern can then receive greater attention during lead identification and biochemical or therapeutic investigation.
The uninhibited control establishes the enzyme’s reaction rate in the absence of the candidate inhibitor. Comparing treated reactions with that reference allows reduced catalytic activity to be evaluated relative to the corresponding uninhibited condition, rather than interpreted from an isolated rate. This comparison provides the basis for identifying an inhibitory effect in the assay.
An initial reduction in activity can lead to more informative follow-up measurements. Investigators may examine concentration-response behavior, estimate an IC50, classify the apparent inhibition pattern, and compare effects across related enzymes. Together, these results distinguish compounds that merely show activity from those with characteristics that justify prioritization as lead molecules.
The approach is useful when researchers need to identify compounds that reduce the activity of a disease-relevant or otherwise important enzyme. Screening can reveal initial lead compounds, provide quantitative inhibition information, and support selectivity assessment. These findings help decide which molecules warrant deeper therapeutic evaluation or further biochemical study.