Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Medicinal chemistry > Dugga 1 > Flashcards

Dugga 1 Flashcards

You may prefer our related Brainscape-certified flashcards:
Periodic Table flashcards Chemistry 101 flashcards AP® Chemistry flashcards Organic Chemistry 101 flashcards
1
Q

What do agonists do?

A

mimic the natual ligand

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What do antagonists do?

A

Bind to the receptor but do not activate it

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Do antagonists bind to regions of the receptor that are not involved in binding the natural ligand?

A

Yes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What do partial agonists do?

A

They induce a weaker effect than a full agonist

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is an inverse agonist?

A

Acts as an antagonist and also eliminate any resting activity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What is desensitisation?

A

When an agonist is bound to its receptor for a long time

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is sensitisation?

A

When an antagonist is bound to a receptor for a long time, the cells synthesise more receptors to counter the effect

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What is tolerance?

A

When an increased dose is required over time to achieve same effect

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What is dependence?

A

The body’s ability do adapt to the presence of a drug

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is pharmacodynamics?

A

How drugs interact with their targets to produce a pharmacological effect

“What the drug does to the body”

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What is pharmacokinteics?

A

The study of factors that affect the ability of the drug to reach its
target in the body

“What the body does to the drug”

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is affinity?

A

A measure of how strongly a drug binds to a receptor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What is efficacy?

A

A measure of the effect of the binding of a drug on the cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What is potency?

A

How effective a drug is in producing a cellular effect

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What sorts of molecules do transport proteins transport?

A

Polar molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What can drugs that target viral structural proteins do?

A

Prevent viruses from entering the cell and inhibit the uncoating

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What is tubulin?

A

A structural protein crucial to cell division and mobility

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What do vinca alkaloids do to tubulin?

A

Bind and inhibit the polymerisation process

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What does paclitaxel do to tubulin?

A

Bind and accelerate polymerisation by stabilising resulting microtubules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

How does a drug targeting lipids work?

A

Disrupting the lipid structure of cell membranes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What do tunelling molecules and ion carriers do to the plasma membrane and to the cell?

A

They result in uncontrolled movement of ions across the cell membrane leading to cell death

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

What is valinomycin?

A

A cyclic structure with alternating ester and amide bonds and acts as a ion carrier

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

What is the definition of a drug target?

A

A macromolecule that has a binding site where the drug binds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

How do drugs bind their target?

A

Intermolecular bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Where do hydrogen bonds occur?

A

Between an electron rich heteroatom and an electron deficient hydrogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

What are hydrophobic interactions?

A

The displacement of ordered layer of water molecules that surround hydrophobic regions. This increases entropy.

27
Q

What needs to happen to polar groups before intermolecular interactions can take place?

A

They have to be desolvated

28
Q

What is the primary structure?

A

The order in which amino acids are linked together

29
Q

What is the secondary structure?

A

Regions of ordered structure within the protein such as alpha helices, beta pleated sheets and beta turns

30
Q

What is the tertiary structure

A

The overall three dimensional shape, how the alpha and beta regions are ordered and linked by interactions

31
Q

What is he quarternary structure?

A

Proteins containing two or more subunits, how the subunits are arranged

32
Q

How are the structures determined?

A

To maximise the favourable intramolecular and intermolecular bonds and minimise unfavourable interactions

33
Q

Where are the polar residues typically favoured?

A

On the outside of the protein because this allows for interactions with water

34
Q

What is proteomics?

A

The study of the structure and function of novel proteins discovered through genomics

35
Q

What are common drug targets?

A

Transport proteins, enzymes and receptors

36
Q

What do transport proteins do?

A

Transport essential polar molecules across the hydrophobic cell membrane

37
Q

What is tubulin?

A

A structural protein crucial to cell division and mobility

38
Q

How does a substrate bind to an active site?

A

With intermolecular bonds

39
Q

When a substrate binds in an enzyme, the shape of the active site may change to maximise binding interactions and in this process what may happen to the bonds in the substrate?

A

It may weaken crucial bonds

40
Q

The amino acid histine is often present in the active site, what does it do?

A

It acts as an acid/base catalyst

41
Q

The amino acid histine is often present in the active site to act as an acid/base catalyst, which other amino acids may be present?

A

Glutamic acid, aspartic acid, tyrosine

42
Q

Which amino acids act as nucleophiles in the reacton mechanism of some enzymes?

A

Serine and cysteine. In some enzymes lysine

43
Q

What are cofactors?

A

Metal ions or small organic molecules. They can be viewed as the body’s chemical reagents.

44
Q

What is a prothetic group?

A

A cofactor bound covalently to an enzyme

45
Q

What is an allosteric inhibitor?

A

Binds to a different binding site and alters the shape of the enzyme so that the active site nolonger works. Often involved in feedback control of biosynthetic pathways

46
Q

What is an isozyme?

A

A variation of the same enzyme. Catalyse same reaction but differ in primary structure, substrate specificity and tissue distribution

47
Q

What does the Michaelis Menten equation relate?

A

The rate of an enzyme catalysed reaction to the substrate concentration

48
Q

What is the Michaelis contant equal to?

A

The substrate concentration at which the rate of enzyme catalysed reaction is half of its max value

49
Q

What does G protein coupled receptors activate?

A

G proteins

50
Q

How many transmembrane section does a G protein coupled receptor have?

A

7

51
Q

Where is the C and N terminals located in a G protein coupled receptor?

A

The C terminal is within the cell and the N terminal outside the cell

52
Q

Receptor types have subtypes. Is it possible for a drug to target only one subtype of the receptor?

A

Yes

53
Q

Intracellular receptors are located within the cell and are important in controlling…

A

transcription

54
Q

How does a chemical messenger for an intracellular receptor pass through the cell membrane?

A

It must be sufficiently hydrophobic

55
Q

What does a G protein consist of?

A

3 protein subunits of which the alpha one is bound to the G protein

56
Q

What happens to the G protein coupled receptor when a ligand binds?

A

GDP is exchanged for GTP which the G protein fractions into an alpha subunit and a beta gamma subunit

57
Q

What does the alpha s subunit bind to?

A

Adenylate cyclase catalysing the formation of cAMP from ATP

58
Q

What does the alpha i subunit do?

A

Inhibits adenylate cyclase

59
Q

What does cAMP do?

A

Acts as a secondary messenger and activates PKA

60
Q

What does PKA do?

A

It catalyses the phosphorylation of serine and threonine residues in other enzymes

61
Q

What are tyrosine kinases?

A

Enzymes that phosphorylate the phenol group of tyrosine. Phosphorylation is a conformational change that affects the activity of the substrate enzyme

62
Q

What do intracellular receptors do?

A

Regulate gene transcription

63
Q
A

Medicinal chemistry (10 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions