Inhibitorconcentratie

Inhibitorconcentratie, or inhibitor concentration in English, refers to the amount of a substance that inhibits a biological or chemical process, typically an enzyme reaction, expressed per unit volume (e.g., micromolar, millimolar) or relative to the concentration of the substrate. The concept is central to enzyme kinetics and drug development, as it quantifies how much of an inhibitor is required to produce a specified reduction in enzymatic activity.

In kinetic studies, inhibitor concentration is combined with models of inhibition to derive constants such as K_i (inhibition constant). For competitive inhibition, increasing inhibitor concentration raises the apparent Km while V_max remains unchanged; non‑competitive inhibition lowers V_max without changing Km; uncompetitive inhibition reduces both parameters. The IC_50 value, the concentration that reduces activity by 50 %, is often used as a practical metric for comparing inhibitor potency across assays.

Measuring inhibitor concentrations involves techniques like enzyme activity assays, fluorescence or absorbance readouts, and more advanced methods such as surface plasmon resonance or isothermal titration calorimetry. Accurate determination of inhibitor concentration is crucial when evaluating the safety of chemicals, environmental pollutants, or potential therapeutics, because off‑target inhibition can lead to adverse effects.

In pharmacology, the inhibitorconcentratie in plasma or target tissues guides dosage decisions and informs pharmacokinetic/pharmacodynamic modeling. High‑throughput screening campaigns routinely calculate inhibitor concentration to prioritize leads. Understanding the relationship between inhibitor concentration, binding affinity, and kinetic parameters enables scientists to design more effective and selective inhibitors for industrial, agricultural, and medical applications.