3 Pharmacodynamics (Ligands)
Pharmacodynamics Overview
Pharmacodynamics: The study of drug effects on the body, specifically how drugs exert their therapeutic effects through mechanisms involving ligands and receptors.
Lecture Structure
Lecture 3 is divided into the following sections:
3.1 Agonists: Substances that activate receptors to produce biological responses.
3.2 Antagonists: Substances that inhibit biological responses by blocking receptors.
3.3 Binding Versus Efficacy: Exploring the relationship between drug binding and its effects.
Learning Objectives
By the end of this section, students should be able to:
Define drug potency and efficacy.
Classify agonists and antagonists based on dose-response curves.
Describe types of antagonists (competitive, non-competitive).
Define allostery and differentiate between drug affinity and efficacy.
Identify receptor reserve from competitive dose-response curves.
Receptor Ligands
Ligands: Substances/drugs that bind to receptors influencing their activity.
Can be classified as:
Agonists: Activate receptors.
Antagonists: Block receptor activity.
Agonists
Definition: Substances that bind to and activate receptors, resulting in a biological response.
Graphical Representation: Concentration-response curves depict efficacy and potency of agonists.
Key terms:
EC50: Effective Concentration for 50% of maximal effect.
Emax: Maximal biological effect observed.
Efficacy vs. Potency
Efficacy: Maximum effect a drug can produce (Emax).
Potency: Concentration dependence of drug effect (related to EC50).
Implication: Strong potency indicates a low EC50; weak potency implies a high EC50.
Variability of Agonists
Agonists can vary in:
Efficacy: Full, partial, or inverse agonists.
Full agonists: Produce maximal effect.
Partial agonists: Generate submaximal effects regardless of dose.
Inverse agonists: Suppress basal activity of receptors.
Antagonists
Definition: Substances that block or inhibit biological responses by binding to receptors without activating them.
Types of antagonists:
Competitive antagonists: Compete with agonists for the same binding site; effects are surmountable at high agonist concentrations.
Non-competitive antagonists: Bind irreversibly or at different sites, reducing agonist efficacy.
Mechanisms of Antagonism
Competitive Antagonism: Requires higher concentrations of agonists to overcome antagonist effects, indicated by a dose ratio.
Schild Plot: A method for evaluating the interaction between agonists and competitive antagonists based on dose ratios.
Partial Agonists as Antagonists
Partial agonists can act as antagonists by competing with full agonists, leading to reduced responses.
This results in a rightward shift (increased EC50) for the full agonist but maintains maximum efficacy (same Emax).
Receptor Reserve
Definition: The availability of receptors beyond what is needed for a maximal biological effect.
In cases of receptor reserve, irreversible antagonists may not reduce maximal biological responses unless concentrations are extreme.
Summary Points
Understanding drug properties requires distinguishing between affinity (how well a drug binds), efficacy (how well it activates), and potency (concentration at which the drug yields effects).
Affinity: Governed by electrochemical properties; high affinity correlates with low KD (equilibrium dissociation constant).
Efficacy: Independent of affinity; measures how well a drug activates its receptor.
The relationship between binding and effect (biological response) is complex.
Next Steps
Prepare for the following lecture on Pharmacokinetics (Part 1).
Contact for questions: Anna Taylor, ataylor1@ualberta.ca.