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Pharmacology > Chapter 1 > Flashcards

Chapter 1 Flashcards

1
Q

1st recorded physician - ancient Egypt

A

Imohtept

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2
Q

What did early pharm look like and how is it different now

A

Early on was looking at how exogenous compounds effected body. Pharmacology started with the recording of physicians. And now today, we are able to look at cellular level and able to do controlled studies to actually tell if a drug is working in a certain way early pharmacology had the possibility of placebo effect.

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3
Q

What did early pharm look like and how is it different now

A

Early on was looking at how exogenous compounds effected body. Pharmacology started with the recording of physicians. And now today, we are able to look at cellular level and able to do controlled studies to actually tell if a drug is working in a certain way

early pharmacology had the possibility of placebo effect.

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4
Q

Who is known as the father of Western medicine?

A

Hippocrates

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5
Q

What was known as the first pharmacology text and as a precursor for the broader pharmacology study?

A

Materia medica

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6
Q

Who is the father of toxicology?

A

Paracelsus. Known for the saying, the dose makes the poison.

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7
Q

Where did the staff symbol originate from to represent medicine?

A

Asclepius-Greek god of medicine he had a rod. It was also confused with Hermes, who also had a rod who is the god of commerce so sometimes those are used interchangeable but not same thing

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8
Q

What is the main difference between modern pharmacology and early pharmacology?

A

The use of regulation allowed for controlled trials to test drug effects and rule out placebo effect

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9
Q

What are the branches of pharmacology?

A

Pharmacodynamics, pharmacokinetics, pharmacogenomics and toxicology

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10
Q

Describe pharmacodynamics:

A

Pharmacodynamics is the drugs effect on the body. For example in a clinical setting you would see those effects (increase HR, BP, etc)

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11
Q

describe pharmacokinetics:

A

What the body does to the drug. For example half-life, does it cross the blood brain barrier?
“ ADME”
Absorption
Distribution
Metabolism
Excretion

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12
Q

Describe pharmacogenomics

A

Specific genetic profile that determines how the body will react to a drug. Different for everyone. Can sometimes use tests to help predict the response before giving a drug.

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13
Q

Describe toxicology

A

The undesirable effects of a chemical on an organism. These are not side effects.

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14
Q

What is the difference between a poison and a toxin?

A

A poison is non-biological whereas a toxin is biological meaning it comes from a living organism (plant or animal). Toxin is a specific type of poison.

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15
Q

What is an agonist?

A

A drug that binds to a receptor to elicit a response.
Usually similar response to endogenous ligand
Agonist can elicit increased or decreased effects

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16
Q

Describe an antagonist

A

A drug that blocks another drug or endogenous ligand from binding to a receptor, So there is no response created.

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17
Q

What is a receptor?

A

A protein on the cell surface. Receptors are made up of chains of amino acids. There are many receptors on each cell.

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18
Q

What makes an organic compound?

A

Must be a carb, lipid, protein, or nucleic acid

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19
Q

What are inorganic compounds?

A

Compounds that do not have carbon, hydrogen, or oxygen as part of their make up

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20
Q

Why is drug size important?

A

If a drug is too big, it may not be able to pass through barriers. It’s important to consider because it may change drug delivery route.
If too small it won’t bind with enough affinity (shape will be off)
For example, would maybe need to give IV if it’s too big to pass through G.I.

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21
Q

Describe how a drug and receptor bind:

A

A drug has a specific shape that binds to the receptor of that shape. It only fits one receptor. “Lock and key”

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22
Q

What are the different elements of drug structure?

A

Size.
Electrical charge: amino acids on the drug bind to the charge on the receptor.
Shape.
Atomic composition

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23
Q

Describe amino acids:

A

Amino acids are either:
Polar: full or partial charge.
Nonpolar: no charge

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24
Q

Name the different type of bonds and discuss strength and specificity of each:

A

Covalent bond: these are the strongest bonds because they share an electron. The drug shape does not need to be perfect because the bond is so strong. This means there is less specificity.

Electrostatic bond: these include ionic bonds, hydrogen bonds, Vanderwal’s forces

Hydrophobic bonds: these are the weakest bonds but most numerous. There is no charge at the receptor site. The shape must be perfect to bond so the specificity is higher.

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25
Q

Describe a drug isomer:

A

Same chemical equation, but different molecular shape creating different effect

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26
Q

What is stereoisomerism?

A

Also known as optical isomer. Isomers that are mirror images.

These isomers do not have the same effect.

Applies to more than half of drugs

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27
Q

What is a racemic mixture?

A

Mixing two different isomers of the same drug.

An example of S ketamine, which is four times more potent, combined with R ketamine, which is more toxic (hallucinations) to form a common racemic ketamine

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28
Q

What are some downsides to racemic mixtures and isomers?

A

Toxic side effects are usually caused by isomers

Purified drugs, reduce negative side effects

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29
Q

What is orthosteric binding?

A

When the drug binds to the active site on the receptor

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30
Q

What is allosteric binding?

A

When a drug binds somewhere else on the receptor, not the active site

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31
Q

Differentiate between specific and non-specific binding:

A

Specific binding is when the drug binds to the receptor it’s supposed to bind to.
There are only a certain amount of receptors so there is a max to specific binding.

Non-Specific binding is when the drug bind somewhere else in the body. There is an increase in non-specific binding once all of the specific binding is maxed

32
Q

What happens if you continue to give a drug when the receptors are maxed out?

A

Can lead to toxic effects

33
Q

What does drug concentration mean?

A

How much drug is in the bloodstream

34
Q

What is EC50?

A

Concentration of a drug where we see 50% effect

35
Q

What is Bmax?

A

When 100% of receptors are bound

36
Q

What is the kd?

A

Drug concentration when 50% of the receptors are bound

37
Q

When would kd be low?

A

When there’s a high drug receptor affinity so they are tightly bound

Wouldn’t need as much concentration to get to the 50% of receptors bound because there’s a high affinity so it’ll quickly reach that 50%

38
Q

When is kd high?

A

When the drug has low affinity to receptor.

It would take a higher concentration to reach 50% because they are binding loosely to the receptor

39
Q

Why doesn’t kd equal EC 50?

A

A drug can reach 50% effect and have a variety amount of receptors bound. It doesn’t have to be 50% receptors to reach that effect.

40
Q

What is a competitive inhibitor?

A

A drug that competes with the agonist for the same binding site. Delays the response of the agonist, but can be out competed by the agonist with increased doses. A.k.a. surmountable.

41
Q

What is an allosteric activator?

A

A drug when given with an agonist, it enhances the effects of the agonist. It increases the max effect of the drug.

42
Q

What is an allosteric inhibitor?

A

A noncompetitive drug that binds outside of the Active site that blocks the agonist from binding to the active site. Can never be out competed by agonist. Insurmountable.

43
Q

What is therapeutic index?

A

Difference between drug response we want and toxic response

44
Q

What are other terms for downstream inhibitor?

A

Indirect agonist or agonist mimic

45
Q

What is an indirect agonist?

A

Doesn’t bind to active site, but elsewhere in the cell to increase drug response in a downstream effect

Known as downstream inhibitor, because it usually inhibits another compound that’s trying to disrupt the chain for the drug to make its full response

46
Q

What happens to the EC 50 when there is a competitive inhibitor present?

A

That you see 50 will be higher because you have to give more agonist to reach that 50% effect

47
Q

What is an orthosteric insurmountable antagonist?

A

An antagonist that is competitive for the active site so it forms a covalent bond that can’t be broken. Would need a new receptor because the agonist will never be able to bind there.

48
Q

What is a partial agonist?

A

It binds with less affinity than the agonist so only partial response.

Can outcompete competitive inhibitors when continue doses are given

Partial agonist can look like an antagonist when full agonist is present because it is binding to the same site as the agonist so it is preventing binding of the full agonist, and the partial agonist has a decrease effect from the agonist

49
Q

What is physiologic antagonism?

A

When different compounds are binding different receptors in the body, but they’re causing opposite effects so they counteract

Beta vs muscarinic receptors-opposite effects

50
Q

What is constitutive activity?

A

Spontaneous activity of receptors. Receptors Can switch back-and-forth between active and inactive, even when drug isn’t present

Most receptors on cell exist in equilibrium between active and inactive

51
Q

What is constitutive activity?

A

Spontaneous activity of receptors. Receptors Can switch back-and-forth between active and inactive, even when drug isn’t present

Most receptors on cell exist in equilibrium between active and inactive

52
Q

What is an inverse agonist?

A

Drug that favors inactive form of receptor

Is classified as an agonist because it binds and elicits a response but clinically looks like antagonist

It lowers beyond the constitutive activity

53
Q

What does an inverse agonist do to receptor activity?

A

Lowers beyond constitutive activity

54
Q

What does a competitive antagonist do to receptor activity?

A

Maintains constitutive activity level no increases or decreases

55
Q

What does an agonist do to receptor activity?

A

Increases activity

56
Q

What does a partial agonist do to receptor activity?

A

Increases activity

57
Q

List different types of drugs

A

Drugs fall into about 70 groups

58
Q

What causes drugs to interact with their receptors?

A

Size
Electrical charge
Shape
atomic composition

59
Q

What are the different states of drugs?

A

Solid liquid or gas

60
Q

What causes drugs interact with their receptors?

A

Chemical bonds

61
Q

Compare potency and efficacy:

A

Potency is EC 50
Efficacy is Emax

62
Q

Why does a drug only last a certain amount of time?

A

How long the drug binds to receptor

Downstream effect when the drug binds to the receptor —can be all used up

63
Q

What happens when a drug forms a covalent bond with the receptor?

A

Often receptor is degraded

Lead to desensitization

Dampens or shut down signal

64
Q

Why is it important Receptors are selective?

A

Most drugs bind to only one receptor or one receptor type

Drugs that bind to multiple receptors in the body it’s probably not a good thing because the drug would have multiple effects on the body

65
Q

What has to happen to the receptor for a downstream effect to occur?

A

Receptor binds to ligand and receptor than changes— 3-D structure shifts

66
Q

What is an inert receptor?

A

Also known as drug carriers

Binds to drugs, but does not change anything

67
Q

What is the most important drug carrier?

A

Albumin

Blood proteins=drug super highway

68
Q

What happens to the drug when it’s bound to a plasma protein?

A

The drug cannot cross barriers

69
Q

When can a drug cross barriers?

A

When it’s in its Freeform

70
Q

How does plasma protein binding affect dosing?

A

Changes how much of a drug we have to give

Ex: if 90% of the drug is bound to albumin only 10% is free so we will need higher dose in order to see effect

71
Q

Why do we have to consider drugs that are given together?

A

Some drugs will kick other drugs off albumin

Compete for binding site on albumin

If competing for a site, both drugs will have higher free concentration

72
Q

What is albumin and how is it produced?

A

Large protein, thousands of amino acids

Produce through transcription and translation in the liver cell

To binding sites—inert carrier

73
Q

What type of drugs bind to albumin?

A

Mostly acidic drugs

74
Q

What are examples of three different drug carriers?

A

Albumin

Alpha-1 acid glycoprotein

Lipoproteins

75
Q

What type of drugs do alpha acid glycoproteins bind to?

A

Basic drugs

76
Q

What type of drugs do lipoproteins bind to?

A

Neutral drugs

Pharmacology (2 decks)

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