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MedChem > Eustaquio > Flashcards

Eustaquio Flashcards

1
Q

What is the trade name of Captopril?

A

Capoten

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2
Q

What is the indication of Captopril?

A

CV disorders, hypertension

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3
Q

What is a side effect of Captopril?

A

Dry cough

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4
Q

What is the drug class of Captopril?

A

ACE-I

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5
Q

What is the enzyme class of Captopril?

A

hydrolase

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6
Q

What type of hydrolase does Captopril fall under?

A

Matallo protease (Zince Portease)

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7
Q

What is the Mechanistic class of Captopril?

A

Acid-base

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8
Q

What is the trade name of Enalapril?

A

Vasotec

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9
Q

What is the trade name of Lisinopril?

A

Prinivil

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10
Q

What is the trade name of Indinavir?

A

Crixivan

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11
Q

What is the drug class of Indinavir?

A

HIV protease

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12
Q

What is phenotypic screening?

A

it is empirical approach. It relies on the phenotypic measures of responses. You don’t know what you are targeting but you know your desired outcome. Uses cell-based assays or animal models

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13
Q

What is target based screening?

A

molecular approach. Hypothesis driven. Uses high throughput and biochemical assay using an isolated target.

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14
Q

What is a structure-guided drug design?

A

Apart of target based screening. Done to improve hits and usually relays on a Crystal structure. Can be used to make the drug fit into the target perfectly.
High throughput + optimization

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15
Q

What is competitive inhibitors?

A

a substrate that competes with the endogenous substrate. if you have excess of the substrate then you can reverse the inhibition.

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16
Q

What is the difference between uncompetitive vs. noncompetitive inhibitors.

A

Uncompetitive inhibitors uniquely bind to the enzyme substrate complex
Noncompeptive not so picky so it can either bind to the enzyme or to the enzyme susbtrate complex.
BOTH do not compete with the substrate

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17
Q

What is a protease?

A

an enzyme that breaks down proteins and peptides using water (hydrolases). Either uses covalent catalysis or acid-based catalysis

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18
Q

Covalent catalysis involves?

A

Serine, Cysteine and Threonine

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19
Q

Acid-base catalysis involves what?

A

metallo and aspartic acid

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20
Q

What are substrate mimics?

A

They mimic the substrate and target the active site

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21
Q

What are transition state mimics?

A

They mimic the transition site but cannot go on to complete the reaction

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22
Q

What is an example of a substrate mimic?

A

ACE Captopril

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23
Q

What is an example of transition state mimic?

A

Hiv protease

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24
Q

What roles do zinc play in the hydrolysis mechanism?

A
  1. Makes carbonyl group more electrophilic
  2. Makes water more nucleophilic
  3. Stabilizes the carboxylate anion
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25
Q

Is zinc acting as a lewis acid or a lewis base?

A

Its acting as a lewis acid. It accepts an electron

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26
Q

Why is cleavage of an amide bond a difficult task?

A

The pair of nonbonded electrons in the nitrogen can delocalize into the the adjacent carbonyl group making the carbonyl group less electrophillic and resistant to hydrolysis.

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27
Q

What do all protease do?

A

They form a transition state called a tetrahedral intermediate

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28
Q

What is the different type of protease?

A
  1. Convalent, Ser, Cys, and Theronine makes a convalent bond with the tetrahedral intermediate
  2. Acid base involves metallo and aspartic acid making a non-covalent bind with the intermediate
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29
Q

Which of the ACE-I aren’t prodrugs?

A

Captopril, Lisinopril

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30
Q

Which can bind more tightly to the enzyme? Transition state mimic or enzyme mimic?

A

Transition state mimic. It has the highest energy.

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31
Q

What do transition state mimics do?

A

Converts the short lived transition state to a stable thermodynamic state

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32
Q

What are lyases

A

Cleaves a chemical bond without using water or oxidation.
Catalyzes the addition or elimination of a small molecule
Equilibrium reaction that can go both ways

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33
Q

What is carbonic anhydrase?

A

It catalyzes the reversible rxns of co2 and water to bicarbonate and a proton . It drastically speeds up this process.

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34
Q

What is the importance of Carbonic anhydrase to human health?

A
  1. Respiration
  2. Bone resorption
  3. Ionic balance in various tissues
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35
Q

What is CA the drug target for?

A

Glaucoma and edema

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36
Q

What is the normal function of CA?

A

H+ is excreted and bicarbonate is reabsorbed

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37
Q

How does Dozolamide treat glaucoma?

A

The majority of liquid in your eye is bicarbonate. Dozolamide will inhibit bicarbonate from being secreted = decreasing the ocular pressure

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38
Q

What is the Zinc Biochemistry?

A
  1. Zinc as cofactors in enzymes
  2. Structural, finger proteins
  3. Regulation (control of cellular zinc)
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39
Q

What are CAs known as?

A

metalloenzymes ZINC

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40
Q

What are transferases?

A

They move a functional group from one molecule to another.

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41
Q

What is an example of a transferases?

A

kinases

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42
Q

How do transferases work?

A

They transfer a phosphate from atp to an alcohol group. Usually OH on serine, or theronine

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43
Q

What disease involve kinase action

A

Cancer

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44
Q

What is the cause of CML?

A

Too much granules and blast being made not enough WBC is being produced

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45
Q

What is the cause of of CML?

A

It is a genetic disorder causes by a chromosomal translocation.

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46
Q

What new chromosome dose CML make?

A

Philadelphia chromosome that has a fusion protein BCR-ABL

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47
Q

What is BCR-ABL?

A

a mutated version of a tyrosine kinase

48
Q

What happens with BCR-ACL is mutated?

A

It is constantly on so granulocytes and blast proliferation ins uncontrolled ABL kinase cannot turn off

49
Q

Why doesn’t Gleevec have a lot of SE?

A

It is very selective. Only selective for ABL tyr kinase.

50
Q

How does Gleevec work?

A

It binds near the activation loop and prevents ATP from binding. Therefore substrate cannot be P, locking it in the inactive position

51
Q

Why was the second generation drug, Dasatinib invented?

A

To overcome the common resistance. But it does not overcome the Tyrosine to Isoleucine mutation.

52
Q

What is a two-substrate enzyme mechanism?

A

Has two substrate involved: ATP and the substrate that is going to get the substrate group added onto it.

53
Q

What are the two main types of two-substrate enzyme mechanisms?

A
  1. ternary complex

2. ping-pong

54
Q

What is the ternary complex mechanism?

A 
Both substrate (atp and substrate to be p) will bind to the enzyme and there will be a direct transfer of phosphate group. 
Random or ordered
55
Q

What is the ping-pong mechanism?

A

Phosphate is given to the enzyme and then the enzyme gives the phosphate group to the substrate.

56
Q

What do most protein kinases following?

A

Ternary complex mechanism

57
Q

What is a common mutation that can occur with Gleevac? Or cancer resistance?

A

Threonine isoleucine mutation.

58
Q

What is the Thr315I mutation?

A

Usually Thr forms a hydrogen bond with Gleevec, the drug. When Thr is mutated to ISO, there is no longer than hydrogen bond, therefore there is a lost of activity

59
Q

How is dasatinib different from imatinib?

A

It does not block the activation loop

60
Q

What did Ponatinib overcome?

A
  1. Steric hinderance caused by Tyr315I

2. loss of h bond with T315I = LOSS OF ACTIVITY AND AFFINITY

61
Q

What is different with the molecule of Ponatinib?

A

Triple bond making it very planar

62
Q

Why does Ponatinib cause more SE?

A

Because it doesn’t interact directly with the activation loop

63
Q

Will we have Gleevec for every disease?

A

No. CML is one mutation affecting one protein. This makes treatment easier and more effective.
It is an inhibitor. Developing an inhibitor is easier than making a medication that reactivates a dysfunctional protein.This disease has the same variant

64
Q

What is oxidoreductase?

A

Transfer of one electron from one molecule to another.

65
Q

What does the genetic variants in aldehyde dehydrogenates will cause what?

A

flushing, servere hangovers

66
Q

What is the purpose of cholesterol?

A
  1. Required for the structural component of cell membranes
  2. bile acids
  3. steroid hormones
67
Q

Where is cholesterol made?

A

Liver and our diet

68
Q

Why must Cholesterol be carried by lipoprotein across the cell?

A

B/x it is lipophillic

69
Q

What is the difference between LDL and HDL?

A

LDL- low density lipoprotein
HDL- high density lipoprotein
LDL- transports cholesterol to cells
HDL- transports cholesterol to the liver for removal

70
Q

What does a high LDL causes?

A

heart angina
brain strokes
peripheral, leg pain when walking

71
Q

What is the rate limiting step on cholesterol?

A

HMG-CoA reductase

72
Q

What are intrinsically disordered regions?

A

Part of the molecule that are disabled. These disabled regions have high energy state and are able to inter convert between confirmations

73
Q

What moieties do all statins have in common?

A

HMG-COA moieties

Rigid hydrophobic group

74
Q

What kind of inhibitors are HMG-CoA i?

A

Competitive substrate mimic

75
Q

What would happen if you did not do screening first when designing statins?

A

It would be hard because statins are so flexible.

76
Q

How is specificity and tight binding of inhibitors achieved?

A

Bulky groups

77
Q

What is protein turnover?

A

The balance between protein synthesis and protein degradation``

78
Q

Why is protein turnover important?

A

to maintain cellular activity

79
Q

What are the two main pathways of protein turnover?

A

Lysosome

Proteasome

80
Q

What does protein turnover play a major role in?

A

Cell cycle, signal transduction, immunity, stress responsive

81
Q

What are lysosomes?

A

They are small vesicles with acidic lumen. The pH inside is acidic and has a lot of acidic hydrolases

82
Q

If Lysosomes are made of hydrolases, why doesn’t it digest itself?

A

It has a polysaccharide coating that protects itself.

83
Q

What is the coating called

A

Glycocalyx

84
Q

What do lysosomes do?

A

They degrade and digestive materials taken up form outside and inside the cell.

  1. autophagy
  2. endocytosis
85
Q

What is the process of autophagy?

A
  1. Isolation membrane will engulf the cargo
  2. Forms autophagosome
  3. fuses with lysosomes
  4. Degradation
86
Q

What are the roles of Autophagy?

A
  1. house keeping/ cellular homeostasis
  2. starvation response
  3. Cellular remodeling
  4. Microbial infections
87
Q

What is bulk autophagy?

A

It is induced by starvation and it is nonselective, will just engulf everything. Untargeted process

88
Q

What is selective autophagy?

A

Ubquitin tagged

cell structures are tagged. Will only degrade things if they are tagged

89
Q

What are some implications of autophagy dysregulation?

A
  1. Cancer
  2. Neurodegeneration
  3. myopathies
90
Q

How does Chloroquine work?

A

increased the pH inside the lumen of lysosomes. Hydrolases work best at an acidic environment. SO THIS WILL INHIBIT AUTOPHAGY

91
Q

What will happen if the pH is greater than the pkA?

A

Deprotonated

92
Q

What will happen if the pH is lower than the pka?

A

protonated

93
Q

What causes neurodegeneration?

A

toxic protein aggregates build up

94
Q

What is lysosomal storage disease?

A

the accumulation of materials inside the lysosomes that doesn’t get degraded. Usually be mutations in gene that contribute to lysosomal function

95
Q

What is lysosomal storage disease mainly due to?

A

deficiency or mutation in lysosomal hydrolases

96
Q

What is an oprhan drug?

A

It is a drug developed for rare conditions. Regulations aren’t as strict

97
Q

Are orphan drugs a cure for the condition?

A

no it will just slow the progression of the disease

98
Q

What are the treatments for lysosomal storage disease?

A
  1. Enzyme replacement therapy
  2. substrate reduction therapy
  3. Chaperone therapy
99
Q

What are enzyme replacement therapy?

A

give your cells hydrolases. Add tag to them so they can localize to your lysosome. Reduces storage materials

100
Q

What are some disadvantage of ERT?

A
  1. Has to be given as an IV
  2. Some people can’t be reached through the systemic circulation such as bone or brain
  3. immune response to it
101
Q

What is substrate reduction therapy

A

to slow down the production of storage materials instead of degrading it

102
Q

What are some advantage of substrate reduction therapy?

A
  1. can take it orally
  2. do not generate immune response
  3. small so it can cross the blood brain barrier
103
Q

What are some disadvantage of substrate reduction therapy?

A

it is only available for two storage disorders

104
Q

What do Chaperones help do?

A

Help fold proteins to their appropriate confirmation

105
Q

What are some advantage of Chaperone therapy?

A
  1. Can be taken orally
  2. don not generate immune reactions
  3. Potential to cross the BBB
106
Q

What are some disadvantage of chaperone therapy?

A

some mutations are unresponsive

107
Q

What makes lysosomal strorage disorders an excellent candidate for gene therapy?

A

single gene disorder well characterized

108
Q

What kind of proteins do lysosome degrade>

A

long lived proteins

109
Q

What kind of proteins do proteasome degrade?

A

short lived proteins. it must first be tagged by UB then it can be put into the barrol to be eaten up

110
Q

How does UB attach to a substrate?

A

terminal of lys and forming and isopeptide bind with it

111
Q

What are the three enzymes required for tagging?

A
  1. E1 activation
  2. E2 conjugation
  3. E3 ligation
112
Q

What determines if the tagged protein goes to proteasome or autophagy?

A

The number of ub that is attached. It makes a code and a specific UBD will bind to the coded ub.

113
Q

What controls what gets in or out of the proteasome?

A

the regulatory cap. It recognizing only tagged proteins. It is the gate keeper

114
Q

What can pass through the lipid bilayer

A

gas, small, unchanged

115
Q

What are ion channels?

A

A collection of protein domains that together create a water filled pore to allow the passage of ion in responses to a chemical, temperature or mechanical stimuli.

116
Q

What do ion channels do?

A

Use excitable cells to convert mechanical and chemical signals to electrical signals

117
Q

What are excitable cells?

A

neuron, muscles and touch receptors

MedChem (2 decks)

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