Pharmaceutical Chemistry and Drug Design Flashcards
6 cards from real Pharm.D. Doctor of Pharmacy practice questions. Tap to flip, then mark Knew It or Still Learning — missed cards come back until you master them.
Read the first 6 Pharmaceutical Chemistry and Drug Design flashcards as text
Which property is described by the octanol-water partition coefficient (logP)?
Answer: Relative lipophilicity of a compound
LogP measures the relative lipophilicity of a compound by comparing its distribution between octanol (lipid-like) and water phases.
Which chemical modification increases water solubility of a poorly soluble drug during pharmaceutical formulation?
Answer: Salt formation or adding ionizable groups
Salt formation (e.g., converting a weak acid to its sodium salt) or adding ionizable groups significantly increases the aqueous solubility of poorly water-soluble drugs.
In the Biopharmaceutics Classification System (BCS), a Class I drug is defined as:
Answer: High solubility, high permeability
BCS Class I drugs have both high solubility and high permeability, making them the easiest to develop for oral delivery and candidates for biowaiver applications.
Which type of drug-receptor interaction is most easily reversed?
Answer: Ionic/electrostatic interaction
Ionic (electrostatic) interactions are reversible and weaker than covalent bonds, making them the most easily disrupted type of drug-receptor interaction.
Which concept explains why adding a methyl group to a drug can sometimes significantly alter its receptor selectivity?
Answer: Steric effects and the 'methyl magic' phenomenon in medicinal chemistry
In medicinal chemistry, 'methyl magic' refers to the phenomenon where adding a methyl group creates steric interactions that dramatically alter receptor binding selectivity or potency.
Aspirin irreversibly inhibits cyclooxygenase (COX) enzymes through which chemical mechanism?
Answer: Acetylation of a serine residue in the enzyme active site
Aspirin irreversibly acetylates a specific serine (Ser530) residue in the active site of COX-1 and COX-2, permanently blocking arachidonic acid binding.