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Receptor theory is the application of receptor models to explain drug behavior. [1] Pharmacological receptor models preceded accurate knowledge of receptors by many years. [ 2 ] John Newport Langley and Paul Ehrlich introduced the concept that receptors can mediate drug action at the beginning of the 20th century.
When two drugs affect each other, it is a drug–drug interaction (DDI). The risk of a DDI increases with the number of drugs used. [1] A large share of elderly people regularly use five or more medications or supplements, with a significant risk of side-effects from drug–drug interactions. [2] Drug interactions can be of three kinds ...
In this context, the biological target is often referred to as a drug target. The most common drug targets of currently marketed drugs include: [4] [5] [6] proteins G protein-coupled receptors (target of 50% of drugs) [7] enzymes (especially protein kinases, proteases, esterases, and phosphatases) ion channels ligand-gated ion channels
Early forms of the receptor theory of pharmacology stated that a drug's effect is directly proportional to the number of receptors that are occupied. [14] Furthermore, a drug effect ceases as a drug-receptor complex dissociates. Ariëns & Stephenson introduced the terms "affinity" & "efficacy" to describe the action of ligands bound to receptors.
Pharmacology is the science of drugs and medications, [1] including a substance's origin, composition, pharmacokinetics, pharmacodynamics, therapeutic use, and toxicology. More specifically, it is the study of the interactions that occur between a living organism and chemicals that affect normal or abnormal biochemical function. [2]
Taking a more sophisticated approach, receptor reserve is an integrative measure of the response-inducing capacity of an agonist (in some receptor models it is termed intrinsic efficacy or intrinsic activity) and of the signal amplification capacity of the corresponding receptor (and its downstream signaling pathways).
The specificity of drugs cannot be talked about without mentioning the affinity of the drugs. The affinity is a measure of how tightly a drug binds to the receptor. If the drug does not bind well, then the action of the drug will be shorter and the chance of binding will also be less.
These pharmacophore points may be located on the ligand itself or may be projected points presumed to be located in the receptor. The features need to match different chemical groups with similar properties, in order to identify novel ligands. Ligand-receptor interactions are typically "polar positive", "polar negative" or "hydrophobic".