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42 Cards in this Set
- Front
- Back
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Medicinal Chemistry |
The identification synthesis and development of new chemical entities suitable for therapeutic use |
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Pharmacology |
The science of drug action on biological systems |
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Pharmacokinetics |
What the body does to the drug |
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Pharmacodynamics |
What the drug does to the body |
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Drug |
Compound the interacts with biological systems |
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Therapeutic index |
Ratio of the amount of a drug that causes toxicity or death to the amount that causes the therapeutic effect <TI = higher safety TI = TD50/ED50 |
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Lead compound |
A compound that shows biological activity |
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Active principle |
A compound that is isolated from a natural extract in which is principally responsible for the extracts pharmacological activity |
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Goals of drug design? |
- Controlled time of action - Localization/targeting |
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6 sources of lead compounds |
- Natural products Serendipity Clinical observations Random Screening Organic synthesis Rational drug design |
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Why are plants good sources of leads? |
They produce secondary metabolites that act as defenses |
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Combinatorial synthesis vs parallel synthesis |
Combinatorial: produces mixtures of compounds in each test vial Parallel: produces unique compounds in each test vial |
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What is high throughput screening? Why is it important? |
Using technology to quickly synthesize and test candidate compounds Important because it can run up to 50 biochemical tests simultaneously |
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Stages of FDA trials |
1: Healthy volunteers or people with disease or condition; Safety and dosage 2: People with disease or condition; Efficacy and side effects 3: People with disease or condition; Efficacy and monitoring adverse reactions |
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5 main biological targets for drugs? |
Lipids Receptors Enzymes Nucleic acids Carbs |
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How to drugs interact with their biological targets and what do these binding interactions typically involve? |
They interact via IMFs (H-bond, VdW, dipole, ionic) |
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What 2 factors determine the length of time a drug is bound to the target? |
Concentration and imf |
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Explain desolvation penalties |
Polar groups of a drug are solvated prior to binding. Desolvation requires energy, for it to be worth it, the stabilization energy gained from drug-target binding much be greater than the energy cost of desolvation |
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Explain protein structure |
Primary: order of amino acids Secondary: interactions between groups to form alpha-helices or beta sheets Tertiary: overall shape of protein Quaternary: interactions between two polypeptide chains |
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How do enzymes increase reaction rates in the body |
Lower activation energies |
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What are enzymes |
Molecules that catalyze reactions in the body |
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Does an enzyme have an active site or binding site |
Active site |
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What is the difference between lock and key binding and induced fit |
Lock and key can only accommodate molecules that fit perfectly in the active site Induced fit alters the shape of the active site to accomodate different molecules |
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Simple enzyme vs complex enzyme |
Simple: only protein structure Complex: protein structure + cofactor |
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What are cofactors, co-enzymes, and prosthetic groups |
Cofactors are small molecules or elements that facilitate interaction between enzymes and drug molecules Coenzyme and slightly bound then released Prosthetic groups are tightly bound |
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Reversible vs irreversible enzyme inhibitors |
Reversible inhibitors undergo no reaction and can be reversed Irreversible inhibitors undergo reactions and cannot be reversed |
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Allosteric inhibition vs allosteric activation |
AI is when the inhibitor binds to the enzyme and alters the active site to where the substrate cannot interact with it AA is when the substrate cannot interest unless the activator is present |
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What are suicide substrates |
Agents which are converted to irreversible inhibitors by the enzyme catalyzed reaction |
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What are receptors? Where are they found? How do they work? |
Cell membrane-bound proteins which contain a binding site for chemical messengers Messenger binds, creates a signal, change occurs due to signal, messenger leaves |
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Neurotransmitter vs hormone |
Neurotransmitters exist in the synapse Hormones have to travel to their target |
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Agonist vs antagonist |
Agonist mimics the natural messenger to activate receptors Antagonists block receptors from natural messenger |
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What is involved in irresersible antagonism? |
Antagonist is covalently bonded to the binding site Often used in diagnostics |
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Pharmacophore |
The part of a molecule responsible for the therpeuric effect |
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Auxophore |
Everything but the pharmacophore What can be altered without losing therapeutic effect |
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What are SARS? |
Structure activity relationships Functional groups are changed to evaluate the QUALITATIVE changes in therapeutic effect |
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In vitro vs in vivo |
In vitro is tested on the target molecules In vivo in tested on organisms |
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What is homologation |
Lengthening a saturated carbon chain to increase drug potency |
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What is chain branching? |
Adding carbon chains to interfere with binding. Steric hindrance |
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What is docking |
Computer assisted movement of a molecule into its active/binding site on target |
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What is QSAR? |
Mathematical relationship between structure and biological activity |
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What are the variables in the Hansch equation? |
Hydrophibicity Electronic properties Steric properties Polar surface area, dipole moment, rotatable bonds, MW |
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LogP |
Ratio of drug concentration in the organic phase to the ratio of drug concentration in the aqueous phase High logP = affinity for organic (nonpolar) Low logP = affinity for aqueous (polar) |
