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Drew 924 > Block3 Lecture1 > Flashcards

Block3 Lecture1 Flashcards

1
Q

What are the 3 classes of incompatibilities?

A

therapeutic, chemical, physical

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2
Q

Define a therapeutic incompatibility.

A

drug combo with antagonistic or synergistic effects

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3
Q

Define a chemical incompatibility.

A

covalent bond changes in drug or excipient upon reconstitution or mixing prior to administration

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4
Q

Define a physical incompatibility.

A

changes in non-covalent interactions upon reconstitution or mixing prior to administration

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5
Q

Define stability.

A

time during which the drug product retains integrity in terms of quality and chemical identity of API

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6
Q

What are the sites for incompatibility in an administration set?

A

1) solution, 2) additive, 3) y-site, 4) syringe

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7
Q

Define additive instability.

A

instability between drug and minibag solution

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8
Q

define solution instability.

A

instability of drug with infusion solution

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9
Q

define y-site instability.

A

instability between 2 drugs at site of mixing

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10
Q

define syringe instability.

A

instability between 2+ drugs in same syringe

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11
Q

What are common co-solvents?

A

ethanol, glycerin, propylene glycol, low-MW PEG

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12
Q

define co-solvent

A

water-miscible organic solvents that are biocompatible

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13
Q

When mixing a large polyanion with a large polycation, what kinetics would you expect?

A

2nd order

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14
Q

Define chemisorption.

A

formation of a covalent bond upon collision with interface

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15
Q

Define physisorption

A

formation of a noncovalent bond upon collision with surface

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16
Q

What is the typical energy of a covalent bond?

A

50-150 kcal/mol

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17
Q

What is the usual bond energy in physisorption?

A

1-10 kcal/mol

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18
Q

What molecular characteristics maximize physisorption?

A

1) planar, 2) large, 3) amphiphilic, 4) opposite ionization state

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19
Q

What are the therapeutic implications for protein adsorption?

A

1) unclear loss of therapeutic agent, 3) possible alteration of surface, 3) possible alteration of protein

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20
Q

How are adsorbed proteins displaced?

A

ion/pH change or shaking

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21
Q

How can protein adsorption be minimized?

A

1) minimize air/water interface, 2) make solid surfaces as hydrophilic as possible, 3) add an adsorption competitor

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22
Q

Why should solid surfaces be hydrophilic regarding protein adsorption?

A

hydrophobic residues are at the core of protein. If container is hydrophobic, protein more likely to unfold and become an antigen.

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23
Q

Define the Vroman Effect.

A

big proteins displace small proteins at a surface

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24
Q

What are examples of adsorption competitors?

A

surfactants (Tweens & Brijs) or serum albumin

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25
Q

What is HAS

A

human serum albumin

26
Q

What should be the concentration of a HSA to maximize rate of HAS adsorption?

A

1-2% w/v

27
Q

What kind of surface is air?

A

hydrophobic

28
Q

Why is it bad to displace adsorbed proteins?

A

precipitation and antigens

29
Q

What are the characteristics of proteins that maximize adsorption?

A

large, amphiphilic, flexible

30
Q

Describe the characteristics of chemisorption.

A

1) usually only at solid-liquid interfaces, 2) released as different molecule, 3) simple monolayers limits capacity

31
Q

What is an advantage to using glass a container?

A

SiO2 is inert to chemisorption

32
Q

Describe the characteristics of physisorption.

A

1) forms at variety of interfaces, 2) same molecular species when released, 3) multilayers can be formed

33
Q

What factors affect physisorption rate?

A

concentration of drug, number of unoccupied sites

34
Q

What is the volume of a minibag?

A

100 mL

35
Q

What are the various types of vaccines?

A

1) whole virus/microbe (attenuated or dead), 2) selected fraction, 3) synthetic protein

36
Q

What are the components of a vaccine?

A

1) antigen, 2) preservatives, 3) additives, 4) residues from manufacture, 5) adjuvants

37
Q

What are examples of preservatives?

A

phenol, 2-phenoxyethanol, thimerosal

38
Q

What are the functions of additives in vaccines?

A

stabilization of the live, attenuated virus to reduce virulence

39
Q

What are examples of additives in vaccines?

A

1) sugars (sucrose/lactose), 2) amino acids (glycine/glutamate), 3) proteins (gelatin/human serum albumin)

40
Q

In which vaccines are protein additives present?

A

MMR, shingles, rabies

41
Q

Advantages to using sugars as vaccine additives?

A

good if frozen, also good for isotonicity

42
Q

What kinds of manufacturing residues may be leftover in vaccines from manufacture?

A

inactivating agents, cellular components, antibiotics

43
Q

What are examples of inactivating agents used in manufacturing vaccines?

A

formaldehyde & glutaraldehyde

44
Q

What cellular components may be leftover in vaccines from manufacture?

A

chicken egg proteins (allergy), and yeast cells

45
Q

Why are antibiotics used in vaccine manufacture?

A

to prevent overgrowth during egg manufacture

46
Q

What kinds of antibiotics are used in vaccine manufacture?

A

streptomycin b, polymixin, amphoB

47
Q

What is the purpose of adjuvants in vaccines?

A

to potentiate the immune response

48
Q

How do adjuvants stimulate the immune response?

A

1) stimulate APCs and dendritic cells, 2) enhances adaptive immune response by unfolding protein to present epitope

49
Q

What are examples of adjuvants?

A

Al(OH)3, AlPO4, KAlSO4

50
Q

What do adjuvants not do?

A

1) directly induce the immune system, 2) irritate locally, 3) toxic

51
Q

How are parental products degraded?

A

1) hydrolysis, 2) oxidation, 3) photo, 4) deamidation

52
Q

What are common buffers?

A

1) ascorbate, 2) citrate, 3) phosphate, 4) bicarb, 5) acetate - painful

53
Q

What is the appropriate range of refrigerator temperatures according to USP?

A

2-8 degrees C

54
Q

What is the appropriate range of freezer temps according to USP?

A

-20 to -10 degrees C

55
Q

How are lyophilized products reconstituted?

A

with SWFI

56
Q

What drugs are susceptible to photodegradation?

A

nitroprusside, amphoB, furosemide

57
Q

How can deamidation be inhibited?

A

bulky amino acids around Arg to inhibit flexibility and through limiting H2O contact

58
Q

What factors affect hydrolysis?

A

1) pH, 2) temperature, 3) H2O

59
Q

For what temp increase does k double?

A

10 degrees C

60
Q

How can oxidation initiation be blocked?

A

1) limit O2, 2) use iron chelators and neutral pH to reduce co-factor contact, 3) limit H2O, 4) rid free radicles with ascorbic acid, 5) limit contact with light

61
Q

What are the 3 steps of free-radical reactions?

A

initiation, propagation, termination

62
Q

How does wavelength affect photodegradation?

A

shorter wavelength = higher energy = faster degradation

Drew 924 (16 decks)

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