University:
University of Wolverhampton
Course:
4PY019 | Pharmacy
Academic year:

2024
Views:

376

Pages:

2
Author:

Sara

Pharmodynamics - how does the drug interact with the body, inhibits or stimulates a biological process primary protein structure amino acid sequence secondary protein structure regularly repeating local structures stabilized by hydrogen bonds. Common examples: alpha helix and beta sheet tertiary protein structure three-dimensional folding pattern of a protein due to side chain interactions. overall structure of a single protein molecule. quaternary protein structure shape or structure that results from the interactions of more than one protein molecule Agonist drug binds to the receptor and gives a similar response to the endogenous ligands (enhanced cellular activity) Antagonist drug binds to the receptor and does not cause a response (blocks/slows cellular activity) Three types of chemical forces/bonds in drug receptor interactions - covalent - electrostatic - hydrophobic Covalent drug receptor interactions - very strong, essentially "irreversible" - not often found in drug action apart from some cancer therapy and inhibition of certain enzymes - weaker than covalent, more common - Ionic , Ion-Dipole , Dipole-Dipole , H+ Electrostatic drug receptor interactions bonds , Charge-Transfer complexes , Van der Waals forces Ionic interactions - strongest non-covalent interaction between oppositely charged ions Ion-Dipole interactions 1/2 - attraction between an ion and the partial charge of a dipole of the opposite polarity Dipole-Dipole Interactions - a partially positive atom in a dipole is attracted to a partially negative atom in another dipole H+ bond interactions - dipole-dipole interaction where one of the constituents is a hydrogen atom attached to a heteroatom Charge-Transfer complex interactions - lone pair of electrons "shared" with a neighbouring group that has considerable pi character Van der Waals interactions - one carbon in a chain approaches another carbon on a neighbouring chain, causing a perturbation known as an induced dipole. These opposite partial charges then attract one another. - generally weak, driven by tendency of molecules to avoid aqueous environments Hydrophobic drug receptor interactions - when two alkyl chains approach one another, water is excluded from the space in between them, resulting in an increase in entropy, and thus a decrease in energy 2/2