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Biopharmaceutics > 13 - Protein & Peptide > Flashcards

13 - Protein & Peptide Flashcards

1
Q

Example of a protein peptide drug?

A

Insulin

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2
Q

Under 40 amino acids long = _____

A

peptide

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3
Q

Over 40 amino acids long = ______

A

protein

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4
Q

Peptides/Proteins are naturally abundant where?

A

in vivo and in vitro

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5
Q

List some characteristics of peptides/proteins

A
  • low dose
  • specific selectivity
  • biocompatibility
  • biodegradability
  • minimal adverse effects
  • large molecules
  • labile configuration
  • instability
  • special in vivo profile
  • targeting difficulty
  • low overall therapeutic outcomes
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6
Q

Peptides/Proteins can undergo denaturation; give a good example of denaturation

A

boiling eggs

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7
Q

There is 4 phases of denaturation; describe them

A

Primary: uncoiling
Secondary: (??? not in my notes)
Tertiary: starts to interact with itself through H bonding
Quaternary: one protein peptide interacts with another peptide

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8
Q

What is the traditional administration type for proteins/peptides?

A

parenteral

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9
Q

What are some novel administration types for proteins/peptides?

A
  • pulmonary
  • nasal
  • ophthalmic
  • buccal/SL
  • rectal
  • transdermal
  • oral
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10
Q

What factors affect stability?

A
  • pH
  • temp
  • ionic strength
  • freeze/thaw effects
  • organic solvents
  • light
  • oxygen
  • surfactants
  • radiation
  • residual moisture
  • shear forces
  • interfacial adsorption
  • heavy metal ions
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11
Q

What is preformulation?

A

“before formulating” - Kelsey
LOL

taking a look at all the characteristics of the drug before formulating it

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12
Q

What factors are taken into consideration in preformulation?

A
  • structure
  • molecular weight
  • pH solubility
  • pH conformation
  • air-water interface
  • freeze/thaw effect
  • solvent compatibility
  • degradation
  • melting point
  • absorbance spectra
  • solvate formation
  • polymorphism
  • hygroscopicity
  • stability tests
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13
Q

What characteristics do you want for in vivo performance?

A
  • various sites from different enzymes
  • quick degradation and metabolism
  • short half-life
  • reach action site with minimal destruction
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14
Q

Describe conventional parenteral dosing

A
  • feasible/practical
  • easy processing
  • low unit cost
  • instability
  • bioavailability deficiency
  • drug targeting difficulty
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15
Q

Describe novel parenteral dosing

A
  • feasible/difficult
  • improved stability
  • potential site target
  • better bioavailability
  • complex processing
  • high unit cost
  • large-scale production difficulty
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16
Q

Anything over ____ microns would usually get stuck in the back of the throat

A

10

17
Q

Describe pulmonary absorption

A
  • systemic absorption and action
  • fast absorption
  • fast onset of action
  • relatively large absorption area
  • relatively mild absorption environment
  • relatively acceptable approach
  • relatively feasible production
18
Q

_____ is currently being processed to be able to be inhaled instead of injected

A

insulin

19
Q

List some surfactants

A
  • tween
  • span
  • sodium laurel sulfate
  • glyceryle monostearate
20
Q

Why do we need an excipient to enhance absorption of peptides/proteins administered rectally?

A

because the protein is so large

21
Q

Describe vaginal application of proteins/peptides

A
  • provides sustained drug action
  • similar to SC implant
  • has shown significant regression of tutors in rats
22
Q

Advantages of oral administration of proteins/peptides

A
  • convenient

- non-invasive

23
Q

Barriers to oral administration of proteins/peptides

A
  • extreme environment
  • extensive metabolism
  • various absorption barriers (pH, enzymes, food)
  • difficult drug targeting
  • cost
24
Q

List some strategies to improve peptides into an oral drug dosage form

A
  • protectant so enzymes don’t get at it
  • structure modification
  • absorption enhances
  • protease inhibitors
  • controlled drug release
  • specific site targeting
25
Q

Describe structure modification

A
  • conjugates
  • prodrugs
  • pH resistant structure
  • enzyme resistant structure
  • balance between hydrophilic and lipophilic properties
26
Q

Describe absorption enhances

A
  • absorption facilitator
  • surfactants or other macromolecules
  • disturbance of normal GI structures
  • potential pharmacologic activity
  • potential interactions
  • long-term toxicity/side effects

*surfactant = most common

27
Q

Describe protease inhibitors

A
  • absorption facilitator
  • macromolecules that deactivate enzymes
  • physical/chemical incompatibility
  • possible total function shutdown
  • risk/benefit evaluation
  • highly controversial and used with caution
28
Q

Describe controlled drug release

A
  • structure protector
  • various established polymers and techniques
  • no adverse effects
  • more effective together with other strategies
29
Q

Describe specific site targeting

A
  • mostly theoretical
  • external guidance to or retention on target (mostly local target)
  • no adverse effects
  • assessment of in vivo effectiveness
  • more effective in combination with other approaches
30
Q

What are some different preparations?

A
  • liposomes
  • microemulsions
  • microcapsules/microspheres
  • bioadhesive formulations
  • solid formulations

Biopharmaceutics (4 decks)

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