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Pharmaceutical Sciences > Biopharmaceutical Exam > Flashcards

Biopharmaceutical Exam Flashcards

1
Q

What are three factors decreasing GI absorption of protein drugs?

A
  1. size limits epithelial permeability
  2. chemical hydrolysis
  3. enzymatic proteolysis
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2
Q

What are two factors affecting protein toxicity (safety)?

A
  1. dose-related pharmacological activity

2. off-target toxicity related to immunogenicity of protein

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3
Q

When does aggregation occur?

A

denaturing leads to exposed hydrophobic residues that can associate with other protein molecules

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4
Q

What are four (4) processes that can cause denaturation?

A
  1. temperature
  2. surface interaction
  3. agitation
  4. foaming
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5
Q

Name five (5) excipients used in biopharmaceuticals?

A
  1. Tween 80
  2. albumin
  3. sucrose
  4. EDTA
  5. TRIS
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6
Q

Why is Tween 80 used in biopharmaceuticals?

A

surfactant and stabilizer against aggregation

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7
Q

Why is albumin used in biopharmaceuticals?

A

protein and stabilizer against surface-mediated aggregation

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8
Q

Why is sucrose used in biopharmaceuticals?

A

diasaccharide used to stabilize lyophilized protein formulations

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9
Q

Why is EDTA used in biopharmaceuticals?

A

metal ion chelator used to protect against oxidative instability

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10
Q

Why is TRIS used in biopharmaceuticals?

A

buffer used to control pH

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11
Q

What is the major limitation of using prokaryotic cells for protein production rather than eukaryotic cells?

A

prokaryotic cells are incapable of post-translational protein modification (e.g. glycosylation)

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12
Q

Why are protein drug substances frozen?

A

Bulk protein drug substance are frozen to stabilize before final drug product formulation.

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13
Q

What are the pros and cons of freezing (frozen liquid) vs freeze-drying?

A
  1. Freezing is less time-consuming
  2. Freezing is less costly
  3. Freeze-drying provides greater stability.
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14
Q

What are two (2) reasons protein drug substanced are lyophilized [freeze-dried]

A
  1. protect against hydrolysis [chemical]

2. protect against physical instability from solutoin [physical]

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15
Q

List seven (7) sources of biopharmaceutical contamination

A
  1. particulates
  2. leachables
  3. bacteria
  4. mycoplasma
  5. virus
  6. pyrogens
  7. endotoxins
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16
Q

List the advantages and disadvantages of live attenuated vaccines

A
  1. adv: possibility of life-long immunity

2. disadv: revert to virulent form

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17
Q

List the advantages and disadvantages of inactivated (killed) vaccines

A
  1. adv: no risk of reversion

2. disadv: require booster administration and adjuvants

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18
Q

List five (5) types of vaccines

A
  1. subunit vaccine
  2. polysaccharide
  3. recombinant
  4. live-attenuated
  5. inactivated
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19
Q

List an example of a subunit vaccine

A

Pertussis

20
Q

List two (2) examples of a polysaccharide vaccine

A
  1. streptococcal pneumonia

2. typhoid

21
Q

List two (2) examples of a recombinant vaccine

A
  1. hepatitis B

2. HPV (papilloma)

22
Q

List eighth (8) examples of live-attenuated vaccines

A
  1. oral polio
  2. measles
  3. mumps
  4. rubella
  5. influenza
  6. smallpox
  7. typhoid
  8. anthrax
23
Q

List five (5) examples of inactivated vaccines

A
  1. cholera
  2. pertussis
  3. inactivated polio
  4. influenza
  5. hepatitis A
24
Q

What is the antigen production host for a viral vaccine?

A
  1. Cell cultures

2. Eggs (chicken)

25
Q

What is the antigen production host for a bacterial vaccine?

A
  1. bacterial fermentation

2. yeast fermentation

26
Q

What are two (2) reasons adjuvants are used in vaccine formulations?

A

enhance immune response by:

  1. increasing antigen uptake
  2. inducing the production of cytokines and complements
27
Q

What is thimerosal?

A

mercury-containing microbial preservative that has historically been used in vaccines

28
Q

What are the safety concerns for thimerosal?

A

potential toxicity in children

29
Q

From what vaccines was thimerosal removed?

A

Vaccines recommended for children – single-dose vaccines.

30
Q

In what vaccines does thimerosal remain?

A

Multi-dose vaccines, including influenza.

31
Q

What is the function of gelatin in vaccinations?

A

stabilize vaccine against physical instability

32
Q

What are the safety concerns of gelatin?

A

one in 2 million children experience hypersensitivity reaction to gelatin

33
Q

What three (3) amino acids are basic?

A
  1. Arginine
  2. Lysine
  3. Histidine
  4. terminal amines
34
Q

What two (2) amino acids are acidic?

A
  1. Aspartic acid
  2. Glutamic acid
  3. terminal acids
35
Q

What amino acids are susceptible to oxidation?

A
  1. Methionine

2. Cysteine

36
Q

What amino acids are susceptible to carbonyl amine reactions (e.g. glycation)?

A
  1. Lysine

2. Terminal amines

37
Q

What amino acids are susceptible to deamidation?

A
  1. asparagine

2. glutamine

38
Q

How does a second structure in a region of “susceptible to degradation” affect rate of degradation?

A

Secondary structure decreases rate of degradation.

39
Q

What is the primary structure?

A

Sequence of amino acids

40
Q

What is secondary structure?

A

Alpha helices and Beta-sheets – amino acid configuration; weak interactions.

41
Q

What is tertiary structure?

A

three dimensional globular sturcture, native and denatured conformations

42
Q

What is quaternary structure?

A

intermolecular interactions such as aggregation and association (dimers, hexamers, polymers)

43
Q

Describe the general trend of protein solubility?

A

Proteins tend to be ionized at extreme pH. There is a certain pH that is the “isoelectric point,” at which net charge is zero and solubility is at minimum.

44
Q

What are three benefits of directions of use in protein pharmaceuticals?

A
  1. avoid aggregations/precipitations problems (temperature, surface interaction, foaming, agitations etc.)
  2. avoid chemical instability
  3. avoid incompatibilities
45
Q

What are three (3) strategies for preventing proteins from degrading?

A
  1. refrigeration
  2. freeze-drying
  3. placing a nitrogen headspace over a drug in a tightly sealed container
46
Q

What are four (4) examples of physical instability?

A
  1. insolubility
  2. foaming
  3. catastrophic aggregation
  4. gelation
47
Q

Does dissolving a protein in D5W increase protein stability?

A

No.

Pharmaceutical Sciences (9 decks)

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