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CHEM 1151 > What is a Drug? > Flashcards

What is a Drug? Flashcards

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1
Q

what are drugs?

A

a compound that interacts with a biological molecule, triggering a physiological effect.

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2
Q

what are a few examples of drugs?

A

morphine, snake venom, herion, LSD, caffeine, penicillin, sugar

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3
Q

what defines a ‘good drug’?

A

good drugs should do what they are meant to do

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4
Q

what does morphine do?

A

pain relief, but can kill you

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5
Q

what does LSD do to you?

A

cause hallucinations

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6
Q

what does caffeine do to you?

A

wakes you up

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7
Q

what does penicillin do?

A

kills bacterial cells

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8
Q

what does sugar do as a drug?

A

is a sense of taste

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9
Q

what can drugs be viewed as?

A

can be viewed as actual or potential poisons

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10
Q

what is selective toxicity?

A

many drugs are effective as they are toxic to ‘problem cells’ but not normal cells

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11
Q

what is therapeutic index?

A

measure of a drug’s beneficial use at a low dose, compared to its harmful effects at a high dose

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12
Q

is a higher or lower ratio better for a drug’s therapeutic index?

A

higher ratio (beneficial use at a low dose:harmful effects at a high dose)

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13
Q

is a higher or lower ratio better for a drug’s therapeutic index?

A

higher ratio (beneficial use at a low dose:harmful effects at a high dose)

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14
Q

why should drugs work?

A
  • the human body is a ‘chemical factory’ (made up of chemicals)
  • drugs enter a system with chemical systems which they interact with
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15
Q

how can drugs have such specific effects?

A

a result of where they act in the body - drug targets

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16
Q

what are drug targets?

A

a molecule in the body that is associated with a particular disease process which can be addressed by a drug to produce a desired therapeutic effect

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17
Q

what must drugs act on?

A

since life is made of cells, drugs must act of cells

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18
Q

what do different drugs act on?

A

different drugs act on different locations of the cell

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19
Q

what are the chemicals in cells?

A

lipids, carbohydrates, proteins and nucleic acids

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20
Q

what are proteins?

A
  • compounds composed of carbon, hydrogen, oxygen and nitrogen
  • arranged as strands of amino acids
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21
Q

what are nucleic acids?

A

naturally occurring chemical compounds that serve as the primary information-carrying molecules in cell

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22
Q

what role do nucleic acids play?

A

directing protein synthesis

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23
Q

what are the two main types of nucleic acids?

A

DNA & RNA

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24
Q

what are the two main types of nucleic acids?

A

DNA & RNA

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25
Q

what makes a molecule a macromolecule?

A

molecular weight in the 1000s of atomic mass units (amu)

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26
Q

what is the process called when drugs interact with a macromolecular target?

A

binding

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27
Q

what is binding?

A

the process of when a drug interacts with a macromolecular target

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28
Q

what is a binding site?

A

a specific area of macromolecule where binding takes place

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29
Q

what form does a bindng site usually take?

A

form of a hollow or canyon

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30
Q

what bonds are involved during binding?

A

intermolecular bonding

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31
Q

what occurs during binding?

A

equilibrium takes place between the drug being bounded and unbounded

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32
Q

what are binding groups?

A

functional groups present in the drug important for forming intermolecular bonds with the binding site

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33
Q

what are binding regions?

A

functional groups present in the target (to bond with the binding groups of the drug)

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34
Q

what is the strongest bond in binding?

A

ionic bonds

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35
Q

where do the ionic bonds form during binding?

A

takes place between groups having opposite charges

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36
Q

are ionic bonds stronger in hydrophobic or hydrophilic?

A

hydrophobic environment

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37
Q

what is the most important initial interaction as the drug enters the binding site?

A

the ionic bonding!!

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38
Q

how do hydrogen bonds occur during binding?

A

normally takes place between an electron-rich heteroatom and an electron (deficient hydrogen)

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39
Q

what two things are essential in hydrogen bonding during binding?

A
  • hydrogen bond donor

- hydrogen bond acceptor

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40
Q

what are the two key classes of functional groups for hydrogen bonding?

A
  • HBA

- HBD

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41
Q

what does HBA refer to in key functional groups for hydrogen bonding?

A
  • carboxylates
  • phosphates
  • ethers
  • alcohols
  • amides
  • amines
  • ketones
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42
Q

what does HBD refer to in key functional groups for hydrogen bonding?

A
  • ammonium ions
  • amines
  • alcohols
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43
Q

what are the weakest bondings in binding?

A

van der waals and hydrophobic interactions

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44
Q

where do van der waals and hydrophobic interactions occur?

A

between 2 hydrophobic regions

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45
Q

what is the strength of van der waals and hydrophobic interactions influenced by?

A

distance between the molecules

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46
Q

what distance is optimal between the drug and binding site to work?

A

as close as possible for it to be important

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47
Q

why are van der waals and hydrophobic interactions important, even though they are weak?

A

there are so many of these interactions that their overall contribution can be significant

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48
Q

what shape are sp^3 hybridised carbons?

A

tetrahedral

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49
Q

how many bonds do sp^3 hybridised carbons have?

A

4 single bonds

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50
Q

when drawing a 3-D molecule, are dashed bonds in front or behind the page?

A

behind

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51
Q

when drawing a 3-D molecule, are wedged bonds in front or behind the page?

A

in front

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52
Q

what is an important factor to a molecules reactions and properties?

A

its shape!

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53
Q

what is shape of a molecule dependent on?

A
  • bond angles

- bond lengths

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54
Q

what is hybridisation of atoms in a molecule?

A

concept of mixing atomic orbitals to form hybrid orbitals

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55
Q

what orbitals does sp^3 consist of?

A
  • one ‘s’ orbital

- three ‘p’ orbitals

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56
Q

what shape does the ‘s’ orbital take?

A

spherical shape

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57
Q

what shape does the ‘p’ orbital take?

A

dumbbell shape

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58
Q

how many orientations of the ‘p’ orbital are there?

A

three

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59
Q

what are the three orientations of the ‘p’ orbital?

A
  • x-axis (Px)
  • y-axis (Py)
  • z-axis (Pz)
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60
Q

which way does Px point?

A

behind page to front of page

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61
Q

which way does Py point?

A

left to right

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62
Q

which way does Pz point?

A

up to down

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63
Q

how does sp^3 form a tetrahedral shape?

A

sp^3 hybrid orbitals have the large lobe of each orbital pointing towards a vertex of a tetrahedron

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64
Q

what is the molecular shape of CH4?

A

tetrahedral

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65
Q

what is the molecular shape of NH3?

A

trigonal pyramidal

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66
Q

what is the molecular shape of water?

A

bent

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67
Q

how does CH4 have a tetrahedral shape?

A

overlapping of four sp^3 orbitals

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68
Q

what are isomers?

A

molecules with the same formula but different atom connections

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69
Q

what is an example of isomerism?

A

butane & 2-methylpropane

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70
Q

why is structural formulae preferred?

A

molecular formulae is inadequate when there are isomers!

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71
Q

what is affected by isomerism?

A

both physical and chemical properties

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72
Q

what are the two types of isomers?

A
  • structural isomers

- stereoisomers

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73
Q

what are structural isomers?

A

isomers with different order of attachment of atoms in their molecules

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74
Q

what are stereoisomers?

A

isomers with the same order of attachment of atoms in their molecules, but different orientation of their atoms/groups in space

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75
Q

what are structural isomers also known as?

A

constitutional isomers

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76
Q

what does structural isomerism cause?

A

different physical and chemical properties

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77
Q

what are examples of structural isomers?

A

2-methylpentane, 3-methylpentane and 2,3-dimethylbutane

all are C6H14

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78
Q

what is functional group isomerism?

A

when structural isomers have different functional groups

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79
Q

what is an example of functional group isomerism?

A

ketones and aldehydes

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80
Q

what are enantiomers?

A

a stereoisomer that is non-superimposable with its mirror image

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81
Q

what does non-superimposable means?

A

can be distinguished from one another (not an exact mirror image)

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82
Q

what does chiral mean?

A

an object which is non-superimposable with its mirror image

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83
Q

what does it mean to be achiral?

A

symmetrical - superimposable

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84
Q

what is plane of symmetry?

A

an imaginary plane passing through an object dividing it such that one half is the mirror image of the other half

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85
Q

how can you test for chirality?

A

does the object posses a plane/s or symmetry?

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86
Q

can molecules be chiral/achiral?

A

yes!

87
Q

how can molecules be achiral?

A

must posses a plane of symmetry

88
Q

what is an example of an achiral molecule?

A

H2Br2

89
Q

what is the structural requirement for molecular chirality (non-superimposable)?

A
  • a carbon atom with four DIFFERENT atoms/groups
  • leads to a molecule that is non-superimposable with its mirror image
  • results in a pair of enantionmers
90
Q

what is a stereocentre?

A

the central carbon atom in a chiral molecule

91
Q

why are molecules with a stereocentre non-superimposable with their mirror image?

A
  • has no plane of symmetry

- different stereostructures

92
Q

do enantiomers have the same or different physical and chemical properties?

A

same physical and chemical properties!!

93
Q

what makes enantiomers different?

A
  • direction a solution of each of the enantiomers rotates the plane of plane polarised light
  • interaction of each of the enantiomers with another chiral molecule
94
Q

what is a racemate/racemic mixture?

A

a mixture of both enantiomers

95
Q

do racemates rotate plane polarised light?

A

no

96
Q

what are optical isomers?

A

molecules with the same molecular and structural formula but have non-superimposable images of each other

97
Q

what is optical rotation?

A

when plane polarised light is passed through a solution of a molecule WITH a stereocentre (chiral) the plane of polarised light is rotated

98
Q

how is optical rotation measured?

A

measured using a polarimeter

99
Q

what is measured with a polarimeter?

A

optical rotation!

  • angle ‘a’
  • direction of rotation (+ or -)
100
Q

what are the consequences of chiral interactions of enantiomers?

A
  • can sometime shave different biological effect - (differing tastes and odours)
101
Q

is it possible to not be able to tell enantiomers apart?

A

yes! both enantiomers of camphor have the same smell

102
Q

what are some examples of enantiomer differences?

A
  • limonene: lemon odour - orange odour
  • carvone: spearmint - caraway seeds
  • MSG: no effect - flavour enhancer
103
Q

what is a biological enantiomer example?

A

L-DOPA - Parkinsons’s disease therapy

D-DOPA - no activity

104
Q

what was an enantiomer gone wrong?

A

thalidomide

105
Q

what is the thalidomide story?

A
  • the drug was administered as a racemate (combination of both enantiomers)
  • the effects of the enantiomers was: sedative & relieved morning sickness - birth defects (teratogenic)
106
Q

why was thalidomide bad?

A
  • given as a racemate
  • responsible for over 10 000 birth defects
  • single dose (50 mg) was enough to cause birth defects!
107
Q

what were a few negative effects caused by thalidomide?

A
  • missing or abnormal feet, arms or legs
  • spinal cord effects
  • absent or abnormal ears
  • 40% mortality
108
Q

why is it unsuitable to just administer the good version of thalidomine?

A

in vitro incubation of each enantiomer showed that they interchanged (interconverted) at a physiologic pH

109
Q

what are the steps for the drug discovery process?

A

medical need –> identify target –> discover molecules that interact with target –> optimise properties of molecules to generate drugs –> pre-clinical studies and drug development –> clinical trials –> drug made!!

110
Q

what steps of the drug discovery process is the ‘drug discovery’?

A
  • medical need
  • identifying target
  • discover molecules that interact with target
111
Q

what steps of the drug discovery process is the ‘drug development’?

A
  • optimise properties of molecules to generate drugs

- pre-clinical studies and drug development

112
Q

what do nucleic acids do?

A

store our genetic information

113
Q

what is the role of DNA & RNA?

A

repository of an organism’s entire hereditary information

- regulates the growth and division of cells

114
Q

how was nucleic acid discovered?

A

1869 - DNA isolated from nuclei, acidic molecule named nucleic acid

115
Q

what does ‘double-helix’ refer to?

A

secondary structure of DNA where DNA strands are twisted into a helical form around a common axis

116
Q

what does ‘stacking interactions’ refer to?

A

weak attractive forces in DNA generated by favorable van der waals interactions between adjacent pairs of bases

117
Q

what does ‘major and minor grooves’ refer to?

A

spaces either above or below the planar faces of bases that offer binding opportunities for proteins and small molecules

118
Q

what are the building blocks of nucleic acids?

A

nucleotides

119
Q

what do nucleotides consist of?

A
  • a heterocyclic base
  • a sugar
  • a phosphate ester
120
Q

what is the ‘watson & crick’ DNA model?

A

consists of two anti-parallel strands of DNA, with a sugar phosphate backbone on the outside and bases on the inside

121
Q

is uracil in RNA or DNA?

A

RNA

122
Q

is thymine in RNA or DNA?

A

DNA!!

123
Q

why does DNA use thymine and not uracil?

A

thymine has a greater resistance to photochemical mutation

124
Q

what is a con of thymine synthesis?

A
  • costly (requires the expenditure of ATP)
125
Q

why is uracil not in DNA?

A

‘U’ in DNA is seen as a ‘mistake’ and is repaired (replaced with C) before DNA synthesis continues

126
Q

is RNA more or less stable than DNA?

A

less stable as a polymer

127
Q

why is RNA less stable than DNA?

A
  • DNA carries the genetic information of the cell, and must remain intact during the lifespan of that cell
  • RNA is synthesised when needed
128
Q

what are the two steps of protein synthesis?

A

transcription and translation

129
Q

what is transcription in protein synthesis?

A

process where the information in a strand of DNA is copied onto a molecule of mRNA (messenger RNA)

130
Q

what is translation in protein synthesis?

A

process of translating the sequence of a mRNA to a sequence of amino acids for protein synthesis

131
Q

what are proteins?

A

large biomolecules that occur in every living organism

  • many different types
  • many biological functions
132
Q

what are some examples of proteins?

A
  • structural proteins
  • protective proteins
  • enzymes
  • hormones
  • physiological proteins
133
Q

what are examples of structural proteins?

A
  • collagen

- keratin

134
Q

what are examples of protective proteins?

A
  • venoms
  • blood-clotting proteins
  • antibodies
135
Q

what are examples of enzymes?

A

proteins that catalyse the reactions that occur in living systems

136
Q

what is an example of hormonal proteins?

A

insulin: regulates glucose metabolism

137
Q

what is an example of proteins with physiological functions?

A

haemoglobin

138
Q

what do proteins consist of?

A

made up of many amino acid units linked together by amide bonds in a long chain

139
Q

what are a-amino acids?

A

building blocks for peptides and proteins

140
Q

what do a-amino acids consist of?

A

amine + acid + side chain

141
Q

what does the ‘a’ mean in a-amino acid?

A

location of the amino group relative to the carboxylic acid

142
Q

how are amino acids differed?

A
  • amino acids only differ by the substituent group (side chain) attached to the a-carbon
143
Q

what are the substituents called in an amino acid?

A

side chains!

144
Q

how do amino acids have such great structural and functional diversity?

A

wide variation of side chains

145
Q

what benefit does have a wide variation of side chains have on amino acids?

A

a great structural and functional diversity of amino acids

146
Q

how many amino acids in proteins are considered common?

A

20

147
Q

how many essential amino acids are there?

A

20

148
Q

what are a few classifications of amino acids?

A
  • hydrophobic
  • hydrophilic
  • acidic
  • basic
149
Q

what are the three types of side chains?

A
  • non-polar
  • polar (not charged)
  • polar (charged)
150
Q

are non-polar side chains hydrophobic or hydrophilic?

A

hydrophobic

151
Q

are polar side chains hydrophobic or hydrophilic?

A

hydrophilic

152
Q

what is are examples of a non-polar side chains?

A
  • H (glycine)
  • CH3 (alanine)
  • CH(CH3)2 (valine)
  • CH2CH(CH3)2 (leucine)
  • CH(CH3)CH2CH3 (isoleucine)
  • CH2Ph (phenylalanine)
153
Q

what are examples of a polar but not charged side chains?

A
  • CH2OH (serine)
  • CH(OH)CH3 (threonine)
  • CH2SH (cysteine)
  • CH2CH2SCH3 (methionine)
  • CH2CONH2 (asparagine)
  • CH2-(benzene)-OH (tyrosine)
154
Q

what is an example of a polar and charged side chain?

A
  • CH2CO2H

e. g. aspartic acid

155
Q

what are the 20 common amino acids?

A
  • glycine (gly)
  • alanine (ala)
  • valine (val)
  • leucine (leu)
  • isoleucine (Ile)
  • phenylalanine (phe)
  • serine (ser)
  • threonine (thr)
  • cysteine (cys)
  • methionine (met)
  • asparagine (asn)
  • tyrosine (tyr)
  • aspartic acid (asp)
  • glutamic acid (glu)
  • lysine (lys)
  • arginine (arg)
  • histidine (his)
156
Q

what are examples of polar (charged) side chains which are acidic?

A
  • aspartic acid

- glutamic acid

157
Q

what are examples of polar (charged) side chains which are baisc?

A
  • lysine
  • arginine
  • histidine
158
Q

are amino acids ionic or covalent?

A

ionic compound sunder normal conditions

159
Q

are amino acids acidic or basic?

A

can be either depending on the pH of the solution

160
Q

how are peptides formed?

A

combining two amino acids (bonded together with an amide bond)

161
Q

what are the four classifications of peptides?

A
  • dipeptide
  • tripeptide
  • tetrapeptide
  • polypeptide
162
Q

what makes a dipeptide?

A

2 amino acids + 1 amide bond

163
Q

what makes a tripeptide?

A

3 amino acids + 2 amide bonds

164
Q

what makes a tetrapeptide?

A

4 amino acids + 3 amide bonds

165
Q

what makes a polypeptide?

A

many amino acids + many amide bonds

166
Q

how are proteins related to peptides?

A

proteins are polypeptides that usually contain >100 amino acid residues

167
Q

how many dipeptides can be made from two identical amino acids?

A

only one!

168
Q

what happens when we combine two different amino acids?

A

four possible products may be formed

169
Q

what is an example of combining identical amino acids?

A

gly + gly –> gly-gly

170
Q

what is an example of combining two different amino acids?

A

ala + gly –> gly-gly, ala-ala, ala-gly ,gly-ala

171
Q

why would ala-gly and gly-ala be different?

A

they have differing sequences of amino acid residues as the sequence of of amino acids in a peptide/protein is read from left to right (n-terminus to c-terminus)

172
Q

how many dipeptides can be created through the combination of three different amino acids?

A

A + B + C –> AA, AB, AC, BB, BA, BC, CC, CA, CB

nine in total!!

173
Q

how many different combinations of dipeptides can we make from 20 amino acids?

A

20^2 = 400 possible dipeptides

174
Q

how many possible tripeptides could made with 2 amino acids?

A

A + B –> AAA, AAG, AGA, GAA, GGG, GGA, GAG, AGG

eight in total!!

175
Q

what is the relationship between BAA, AAB and ABA?

A

all isomers with different sequences

176
Q

how many tripeptides can be created using 20 amino acids?

A

20^3 = 8000 possible structures

177
Q

if a protein has 100 amino acid residues, how many possible structures are there?

A

20^100 possible structures

178
Q

what is an example of the importance of sequence in amino acids?

A

sickle cell anaemia

179
Q

what is sickle cell anaemia caused by?

A

substitution of a valine residue by glutamic acid resulting in the change of the shape of haemoglobin

180
Q

what shape do amide bonds take on?

A

planar

181
Q

why is the shape of amide bonds important to protein structure?

A

partial double bond character of the amide bond also has stereoisometric consequences

182
Q

what are the three levels of structure for proteins?

A
  • primary structure
  • secondary structure
  • tertiary structure
183
Q

what does primary structure refer to in proteins?

A

the sequence of amino acids

184
Q

what does secondary structure refer to in proteins?

A

folding of the primary structure into domains (i.e. a-helices, b-sheets)

185
Q

what does tertiary structure refer to in proteins?

A

additional intra-chain interactions such as hydrogen bonding between amide groups/side chain groups and covalent bonds

186
Q

what is the structure of a-helix?

A

coiling of the polypeptide backbone around the long axis of the protein molecule

187
Q

what does ‘steric hindrance’ refer to in a-helix’?

A

r-groups of the a-helix protruding outwards to minimise steric clashing

188
Q

what is steric clashing?

A

unnatural overlapping of any two non-bonding atoms in a protein

189
Q

what is the structure of a b-sheet?

A

the polypeptide backbone forms an extended zigzag structure resembling a series of pleats

190
Q

how do proteins maximise their stability?

A

by folding spontaneously

191
Q

how is free gibbs energy related to protein stability?

A

large negative ∆G = stable protein

every time there is a stabilising interaction between two atoms, free energy is released

192
Q

will proteins fold the polar sections on the inside or outside?

A

proteins will fold so that it exposes the maximum amount of polar groups to water and buries the non-polar groups in the protein interior

193
Q

what is quaternary structure in proteins?

A

3D arrangement of individual peptides within a multisubunit protein

194
Q

what proteins do drugs interact with?

A
  • enzymes: body’s catalysts
  • receptors: crucial for communication between cells
  • carrier proteins: transport chemicals into and out the cell
  • structural proteins
195
Q

what are the main steps for modern drug discovery and development?

A

choose a disease –> choose a drug target –> identify a bioassay –> find a ‘lead’ compound –> identify structure-activity relationships –> identify the pharmacophore and improve target interactions –> improve the pharmacokinetic properties –> patent the drug –> study drug metabolism –> test for toxicity –> design a manufacturing process –> carry out clinical trials –> market the drug

196
Q

what factors must be considered when ‘choosing a disease’ during drug discovery and development?

A

economic and medical factors

197
Q

what is the two most basic classifications when choosing a disease during drug discovery and development?

A
  • first-world diseases
    (e. g. migraine, depression, ulcers, cancer, obesity)
  • third-world diseases
    (e. g. malaria, sleeping sickness)
198
Q

what are the steps to ‘choose a drug target’ during drug discovery and development?

A
  • identify a suitable target (enzyme, receptor, nucleic acid)
  • need to understand the biology of the disease state
199
Q

what does ‘identifying a bioassay’ include during drug discovery and development?

A
  • used to screen compounds to discover ‘leads’
  • in vivo - animal testing
  • in vitro - tissues, cells or enzymes are used
  • screening by NMR spectroscopy (to see if a compound binds to a protein target)
200
Q

what does ‘finding a lead compound’ include during drug discovery and development?

A
  • a ‘lead’ is a compound that displays the desired pharmaceutical activity (starting point for the development of a drug)
201
Q

what does ‘finding a lead compound’ include during drug discovery and development?

A
  • a ‘lead’ is a compound that displays the desired pharmaceutical activity (starting point for the development of a drug)
  • screening of natural products (plants, microbes, venoms/toxins)
  • medical folklore (morphine, cocaine)
  • screening of synthetic libraries
  • existing drugs
  • starting from the natural ligand
  • computer aided design/data mining
202
Q

what are the criteria that must be ticked off for a drug to be successful?

A
  • must be stable (chemically and metabolically)
  • good solubility profile
  • synthetically feasible
  • must be novel (patentable)
  • safe to use
  • effective for the intended use
203
Q

how does ‘stability’ make a drug successful?

A
  • chemical: so the drug doesn’t fall apart before you use it
  • metabolic: survive the various metabolic enzymes of the GI tract/liver (can cause excess liver enzymes which will break down other drugs)
204
Q

how does ‘solubility’ make a drug successful?

A
  • water-soluble: if too little, cannot be absorbed and distributed throughout the body. if too much, will rapidly leave through the kidneys
  • lipid-soluble: if too little, cannot be absorbed across lipid membranes. if too much, may partition to fat stores and not reach intended site of action
205
Q

how does a drug being ‘synthetically feasible’ make it successful?

A
  • starting materials must be readily available

- cheap to make in large quantities

206
Q

how does a drug being ‘novel’ make it successful?

A
  • must be sufficiently novel enough for it to be patented

- requires patent protection to justify money spent to approve drug

207
Q

how does ‘effectiveness’ make a drug successful?

A
  • in vivo - testing on animals to show that it works
  • lots of animal testing before human trials
  • phase i, phase ii and phase iii clinical trials - send paperwork to FDA to be approved
208
Q

how does ‘safety’ make a drug successful?

A
  • large therapeutic index is preferred
    (toxic dose:therapeutic dose)
  • begin with acute toxicity in mice
  • checking for mutagenicity and teratogenicity
  • check for chronic effects over several generations
  • safety tests on several species of animals before human trials
209
Q

what is mutagenicity when determining the safety of a drug?

A

the capacity to induce mutations

210
Q

what is teratogenicity when determining the safety of a drug?

A

prenatal toxicity: structural or functional defects in developing embryos or foetuses

211
Q

what are the three phases in clinical trials testing for drug safety?

A

phase I, phase II, and phase III

212
Q

what does phase I include for clinical trials when testing for drug safety?

A

the compound is tested on healthy volunteers at a range of doses to establish that there are no immediate adverse effects

213
Q

what does phase II include for clinical trials when testing for drug safety?

A

compound is tested on a small number of patients in order to establish that there is a positive effect and what dosage is required to achieve this effect

214
Q

what does phase III include for clinical trials when testing for drug safety?

A

large-scale double-blind trials - compound is compared against an established drug and/or placebo (objective measure of the drug’s effectiveness)

CHEM 1151 (3 decks)

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