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MPharm Stage 1 > Unit 1: Fundamental Chemistry of Drugs and Molecules of Life > Flashcards

Unit 1: Fundamental Chemistry of Drugs and Molecules of Life Flashcards

1
Q

Heteroatom

A

Any atom that is not hydrogen or carbon

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2
Q

How to identify an alcohol (-OH)

A

Polar
Hydrogen bonding
Electronegative
Two lone pairs

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3
Q

How to differentiate between carbonyls (aldehydes and ketones C=O)

A

Aldehyde – if one of the atoms is carbon and the other one hydrogen
Ketone – if both of the atoms are carbons

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4
Q

Where would you find a thiol (-SH)

A

Found in α-amino acid cysteine
Linking peptides through a disulphide (-S-S-) bridge
Lower electronegativity than O Cannot undergo hydrogen bonding to the same extent

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5
Q

Feature of a carboxylic acid (-COOH)

A

Show acidic behaviour – can dissociate to lose a hydrogen ion from the hydroxyl group

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6
Q

How to identify esters (-COO-R’)

A

Formed from carboxylic acids and alcohols by esterification
Note the difference to carboxylic acid group (R’ = alkyl group instead of H)

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7
Q

How to identify amides (–CONR2)

A

Consists of a carbonyl group directly attached to a nitrogen atom
Highly polar
Form strong intermolecular interactions

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8
Q

α-lactam

A

3 atom amide ring

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9
Q

β-lactam

A

4 atom amide ring

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10
Q

γ-lactam

A

5 atom amide ring

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11
Q

δ-lactam

A

6 atom amide ring

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12
Q

ε-lactam

A

7 atom amide ring

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13
Q

Features of an Amines (N’H’3)

A

Derived from ammonia NH3
Can undergo hydrogen bonding
Solutions of amines in water are basic
Soluble in water

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14
Q

What determines the order of priority of functional groups in the suffix of the name

A

The most oxidised functional group in the structure takes precedence when we decide on the suffix.

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15
Q

Order of priority of functional groups

A

Carboxylic acid, ester, acid halide, amide, nitrile, aldehyde, ketone, alcohol, thiol, amine, alkene, alkyne, alkane

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16
Q

amphoteric compound

A

a compound able to react as both an acid and base

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17
Q

pKa

A

the pH at which ionisation of an acid or base is at exactly 50%.
measures how weak or strong an acid is
https://www.youtube.com/watch?v=IQ6gHQAg_Nk

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18
Q

what do pKa values mean in terms of acidity

A

lower pKa value= stronger acid
greater its ability to donate its protons

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19
Q

what do pKa values mean in terms of basicity

A

higher pKa value= stronger base
greater ability to accept protons

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20
Q

orbital hybridisation

A

the concept of mixing these atomic orbitals to form new hybrid orbitals suitable for the pairing of electrons to form covalent bonds in molecules.

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21
Q

Acid

A

H+ donor

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22
Q

Base

A

H+ acceptor

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23
Q

pH

A

pH = -log10[H+]
represent the acidity of a solution – it measures hydrogen ion concentration

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24
Q

An unionised compound is…

A

less soluble in water than in non-polar solvents
more likely to pass through cell membrane than ionized

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25
Q

An ionised compound is…

A

more soluble in water than in non-polar solvents

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26
Q

What does an effective drug need to be in terms of solubility

A

Be sufficiently soluble in water to dissolve in blood plasma and be carried around the body (to reach area where needed) while also being sufficiently soluble in non-polar lipids to pass through cell membranes into cells (and carry out function)

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27
Q

Will an acid be ionised at a pH value higher or lower than its pKa value?

A

pH > pKa
higher pH is more basic, so acid is in its conjugate base form

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28
Q

Will a base be ionised at a pH value higher or lower than its pKa value?

A

pH < pKa
lower pH is more acidic, so base is in its conjugate acid form

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29
Q

conjugate acid

A

species that forms when a base gains a proton

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30
Q

conjugate base

A

species that forms when an acid donates a proton

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31
Q

sigma bond

A

sharing electrons by overlap of an sp2 orbital from each atom forming a strong single bond
electron density concentrated between nuclei

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32
Q

pi bond

A

Overlap of the parallel p-orbitals forms an orbital that places a cloud of electrons above and below the sigma (single) bond

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33
Q

What hybridisation and shape is shown with 4 sigma bonds

A

Hybridisation- sp3
Shape- Tetrahedral

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34
Q

What hybridisation and shape is shown with 3 sigma bonds

A

Hybridisation- sp2
Shape- Trigonal

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35
Q

What hybridisation and shape is shown with 2 sigma bonds

A

Hybridisation- sp
Shape- Linear

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36
Q

Why is a detailed understanding of stereochemistry vital in pharmaceutical science?

A
  • The clinical efficacy of a drug is critically dependent on its three-dimensional structure
  • The stereochemistry of a drug can impact upon its toxicity and side effects
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37
Q

enantiomer

A

structures that are nonsuperposable mirror images of one another

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38
Q

analgesic

A

painkiller

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39
Q

What is the only detectable physical difference between a pair of enantiomeric molecules?

A

their ability to rotate the plane of polarised light,
they are often referred to as optical isomers

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40
Q

What happens if a drug is chiral?

A

Usually only one enantiomer will interact fully with the receptor
Drugs should optimally be administered as single enantiomers

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41
Q

If a drug is chiral, and therefore only one enantiomer is active, what effects can its mirror image isomer have?

A

Inactive
Producing side effects
Countering the effect of the drug
Being metabolised to a toxic product

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42
Q

What do companies do because chiral synthesis or separation can be expensive?

A

Companies market racemic mixtures of synthetic drugs if they can. This can be risky

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43
Q

R enantiomer

A

clockwise

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44
Q

S enantiomer

A

anticlockwise

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45
Q

how to determine whether it is R or S enantiomer

A

Step 1. Assign “priority” to each atom attached to the chiral centre (according to atomic number).

Step 2. View the molecule with the lowest priority (4th) group (often H) directed away from the observer.

Step 3. Observe the order of priority: join the 1, 2, 3 groups together, if the direction is clockwise, the isomer is rectus (R), if anticlockwise sinister (S) (Figure 15).

Step 4. If two or more atoms attached to a chiral centre are the same, look to second and third atoms until it is possible to distinguish between groups. The highest priority different atom takes precedence; you do not add the atomic numbers together.

Step 5. For multiple bonds, treat as single bonds to duplicate or triplicate atoms of the same type.

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46
Q

diastereoisomers

A

are stereoisomers of each other but they are not specifically mirror images of each other

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47
Q

Cis-trans diastereoisomers

A

found in molecules with double bonds and saturated rings

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48
Q

Chiral Diasteroisomers

A

Chiral isomers which are not enantiomers, i.e. not mirror images of each other.

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49
Q

Racemic mixture

A

an equal mixture of both enantiomers of a compound, has no measurable optical rotation

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50
Q

Two types of intermolecular interactions

A

Electrostatic
Hydrophobic

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51
Q

Hydrogen bonding

A

Forms when electronegative N, O, F approach a hydrogen atom covalently attached to another electronegative atom, e.g. between carbonyl and amino group.

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52
Q

Charge-charge interactions/PDD

A

Electrostatic like H bonds but distance between interacting groups isn’t fixed and alignment isn’t as important.
Any group/atom in a molecule which carries a charge (electronegativity difference between atoms the presence of an acidic or basic group, or an atom with a lone pair of electrons)
Can be attractive or repulsive.

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53
Q

What is interactions between charged groups likely to be dependent on?

A

pH-dependent
e.g. with proteins- the carboxyl group loses the proton and the amino group gains the proton

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54
Q

Hydrophobic interactions

A

Hydrophobic groups are insoluble, do not contain any particularly electronegative atoms, e.g. CH3.
– Neutral groups- which have no way of interacting with water.
– Apolar groups do not interact or repel each other, but rather come together through the action of the water solvent

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55
Q

What does an amino acid contain?

A

Contains an acidic group (carboxylic group), basic group (amine), R group, H atom

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56
Q

Why are all standard amino acid classed as “α-amino acids” and what is the exception?

A

They all have an amino group on the first (α) carbon atom adjacent to the carboxylic acid group
They are primary amino acids since they have a primary amine group
Exception is proline- it has a secondary amine group.

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57
Q

Which α-amino acid is not chiral?

A

Glycine

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58
Q

5 groups that amino acids can be split into

A

Non polar (straight or branched chains that may or may not be cyclical)
Aromatic
Uncharged polar
Charged (negative/acidic or positive/basic side chains)
Sulphur containing

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59
Q

How is an amino acid ionised in acidic medium?

A

The carboxylic group is unionised while the amino group is in its ammonium ionised state
Protonated form
<pKa1

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60
Q

How is an amino acid ionised in a basic medium?

A

The carboxylic acid group in its ionised carboxylate form while the amino group is in its non-ionised state
Deprotonated form
>pKa2

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61
Q

When is a zwitterion formed?

A

Around neutral pH
Both groups ionised
Zero net charge

62
Q

6 functions of proteins and an example for each

A

Structural proteins, e.g. collagen
Movement proteins e.g. myosin
Transporter proteins e.g. GLUT family of glucose transporters
Metabolic proteins e.g. hexokinase
Communication proteins e.g. insulin
Defence and protection e.g keratin, antibodies, thrombin

63
Q

Metabolic proteins

A

Enzymes that catalyse the breakdown and synthesis of biological macromolecules to maintain cellular function

64
Q

Hexoknase

A

Converts glucose to glucose-6-phosphate, first step in glycolysis

65
Q

Primary structure

A

the simple linear sequence of amino acids in the polypeptide chain of a protein

66
Q

Secondary structure

A

Local arrangement of amino acids with respect to each other to form defined, hydrogen-bonded structures.

67
Q

Alpha helix

A

H bonds form between Oxygen atom of carbonyl group and NH hydrogen of amine group 4 places down the strand.

68
Q

In alpha helixes. why do the side chains of individual amino acids point outwards?

A

Improves stability of the helix by preventing steric hinderance.

69
Q

B pleated sheet

A

Hydrogen bonds formed between peptide chains lying adjacent to eachother
Parallel sheets occur when these strands run from N to C terminals in the same direction.
Anti-parallel sheets occurs when protein strand folds back on itself

70
Q

Tertiary structure

A

Complex coiling and folding of secondary structure elements that determines the 3D structure of the protein.

71
Q

Quaternary structure

A

Interaction between individual polpeptides to form multisubunit protein complex.

72
Q

Globular proteins, examples and features

A

Have irregular, rounded shape
E.g. myoglobin, haemoglobin, hormones (insulin) and enzymes.
Core typically made of non-polar amino acid residues, outer surface is usually charged and polar.
These proteins are readily soluble in cytoplasm and other aqueous environments
Make use to alpha helixes.

73
Q

Fibrous proteins, examples and features

A

Linear helical or sheet-like structures
Usually due to association of secondary structures (e.g. collagen triple helix)
Or due to quaternary association of several individual sheets (e.g. keratin)
Tough, usually water insoluble, protective or structural role in body

74
Q

How does sickle cell anaemia arise?

A

Due to the substitution of a single amino acid in haemoglobin (termed HgbS) resulting in a mutated haemoglobin with a different primary sequence.

75
Q

What happens to RBC in sickle cell anaemia?

A

Normal RBC are quite elastic, which allows the cells to deform to pass through capillaries.
In sickle-cell disease, low oxygen tension alters the shape of haemoglobin, and promotes RBC sickling (bending to a curved shape) which damages the cell membrane and decreases elasticity.
These cells fail to return to normal shape when normal oxygen tension is restored. Rigid blood cells are unable to deform as they pass through narrow capillaries, leading to vessel occlusion and ischaemia.

76
Q

What is the actual anaemia of the illness caused by?

A

by faster than normal destruction of the red cells because of their altered shape

77
Q

Hydrophobic effect in proteins

A

where non-polar substances combine in aqueous solution, minimising disruption to the hydrogen bonds between water molecules

78
Q

What is a disadvantage of protein crystals (freezing) and what can be added to combat this

A

high molecular weights can make proteins hard to crystallise.
Sugars, such as mannitol and sucrose can be added

79
Q

Disadvantage of proteins being removed from there environment and how to fix this

A

If proteins removed from their environment- activity can be lost. Interactions between hydrophobic amino acid residues can minimised SA exposure to water. Freeze-drying of proteins can enhance their stability and shelf life.

80
Q

DNA

A

Consists of two biopolymer strands coiled around each other to form a double helix
Specific bases (adenine, guanine, thymine and cytosine) interact in defined pairs.
A is always paired with T, and G is always paired with C These interactions occur via hydrogen bonding

81
Q

Transcription

A

Double stranded DNA is transcribed to produce single stranded RNA.
Three major types of RNA (messenger; ribosomal and transfer) are transcribed from DNA and participate in the process of translation Messenger RNA (mRNA) is the type of RNA that carries the genetic code required to make proteins.

82
Q

Translation

A

mRNA is translated into proteins in the cytoplasm on ribosomes.
tRNA carries individual amino acids to the ribosomes, where they are joined in via peptide bonds to form proteins.
During translation, the sequence of nucleic acid bases in mRNA is read in sets of three (each set of three bases constitutes a codon).
The sequence of codons in the mRNA dictates the sequence of amino acids in the protein.
Thus, DNA is said to comprise an organism’s “genetic code”.

83
Q

Biotechnology

A

the use of molecular methods to modify and engineer the genetic material of living cells so they will produce new substances and/or perform new functions

84
Q

Genetic testing

A

medical tests that identify molecular changes in chromosomes, genes, or proteins
e.g. downs syndrome testing, or sickle cell disease testing

85
Q

What is pharmacogenomics

A

an individual patient’s “single nucleotide polymorphisms” can help predict how quickly they will metabolise particular drugs
e.g. the liver enzyme CYP2C19 metabolises several medicines, including the antiplatelet medicine clopidogrel (prodrug)
Some patients possess SNPs in specific places on the CYP2C19 gene that make it a poor metaboliser of Clopidogrel.

86
Q

Where are glycogen and cellulose

A

hese are critical energy stores in animals and plants respectively. In mammals, glycogen is synthesised and stored in liver and skeletal muscle.

87
Q

what is cellulose

A

this is the fundamental structural component of plant cell walls

88
Q

oligosaccharide

A

Carbohydrates of intermediate chain length (between 3 and 10 monomers)

89
Q

differences between β-lactose and α-lactose

A

β-lactose is twice as sweet as α-lactose.
α-lactose has better powderflow properties and therefore is more commonly used as an additive in pharmaceutical industry for tablet production than β-lactose

90
Q

difference between lipid and carbohydrate

A

oxygen content of lipids is much less than that of carbohydrates, meaning that lipids are typically water insoluble.

91
Q

unsaturated

A

double bonded

92
Q

triglyceride

A

3 fatty acid and 1 glycerol

93
Q

strengths of cholesterol

A

Essential for cell membrane fluidity and is a metabolic precursor for bile, the active form of vitamin D and all estrogens.
Cholesterol is transported using special carriers called lipoproteins.
LDL (low density lipoproteins) essentially transport cholesterol from liver and intestine to the rest of the body.
Meanwhile HDLs (high density lipoproteins) remove excess cholesterol and transfer it back to the liver.

94
Q

what is a risk factor for atherosclerosis and cardiovascular disease

A

high levels of LDL cholesterol in the blood

95
Q

what is a class of drug commonly used to reduce LDL levels

A

statins- atorvastatin

96
Q

how does atorvastatin decrease cholesterol production

A

A potent competitive inhibitor of HMG-CoA reductase.
This enzyme plays a pivotal role in producing mevalonic acid, which is an upstream
precursor to cholesterol.
Inhibition of this rate-
limiting step decreases cholesterol production and also the production of a variety of isoprenoids that may have roles in pro-inflammatory signalling

97
Q

Fat soluble vitamins

A

Can be stored long term in the body
Vitamin A, D, E, K

98
Q

Water soluble vitamins

A

Readily excreted
B complex and vitamin C

99
Q

Types of b complex vitamins

A

Vitamin B1/Thiamin
Vitamin B2/Riboflavin
Vitamin B3/Niacin
Vitamin B6
Vitamin B7/Biotin
Vitamin B9/Folic acid
Vitamin B12/Cobalamin

100
Q

Where is vitamin B1/thiamin found?

A

Widespread in both animal and plant kingdoms- in tissues high in carbohydrates/associated with carbohydrate metabolism.

101
Q

What is thiamines free form name?

A

Thiamine diphosphate/thiamine pyrophosphate (TPP)
or as triphosphate.

102
Q

What is thiamine essential for?

A

Carbohydrate metabolism- growth and development.

103
Q

What is a potentially fatal thiamine deficiency disease and what are its symptoms?

A

Beriberi
Weight loss, sensory/cognitive dysfunction, weak/painful limbs, heart problems

104
Q

How does vitamin B2/riboflaxin exist in the body and what is this?

A

Exists predominantly as flavin mononucleotide (FMN) or flavinadenine dinucleotide (FAD)
which are prosthetic groups in a variety of respiratory enzymes involved in energy release

105
Q

What can vitamin B2/riboflavin deficiency lead to and is this common or rare and why?

A

deficiency can lead to ariboflavinosis,
causes stomatitis of the mouth and tongue, cheilosis (chapped and fissured lips) and a scaly rash on the genitalia.

106
Q

What is vitamin B3/niacin name given to?

A

name given to both nicotinic acid and its amide

107
Q

what are good sources of niacin?

A

Meats, fruits and vegetables

108
Q

What is essential for energy metabolism in niacin?

A

occurs in vivo as part of the co-enzymes NAD and
NADP, and is thus essential for energy metabolism

109
Q

What does vitamin B3/niacin deficiency lead to?

A

results in pellagra, the pathological impact of which is broad and results in death if not treated

110
Q

What is the active form of vitamin B6 ?

A

pyridoxal-5-phosphate
exists as a variety of interconvertible forms such as pyridoxine (most common B6 supplement) pyridoxol (only found in plants) and pyridoxamine (only found in foods of animal origin), all of which can also be phosphorylated.

111
Q

where can vitamin B6 be found?

A

Meat, egg yolk, and wheatgerm are abundant sources with less found in milk and cheese

112
Q

What are vitamin B6 molecules prosthetic groups for?

A

B6 molecules are prosthetic groups to a variety of enzymes involved in amino acid/glucose/lipid metabolism, and the synthesis of haemoglobin

113
Q

Deficiency for vitamin B6

A

whilst deficiency symptoms are similar to those for other “Bcomplex” vitamins, anaemia is also possible

114
Q

What is vitamin B7/biotin and what role does it play?

A

Biotin is a prosthetic group in enzymes that play a role in amino acid/glucose/lipid metabolism

115
Q

Is there deficiency with vitamin B7/biotin?

A

Deficiency is rare, but can happen when patients utilise parenteral nutrition (IV) for long periods.

116
Q

What does vitamin B9/folic acid occur as in the diet?

A

as a group of polyglutamyl conjugates

117
Q

sources of vitamin B9/folic acid

A

Liver and leafy green vegetables are good sources

118
Q

active forms of vitamin B9/folic acid in vivo and what are they co-enzymes in?

A

Tetrahydrofolic acid and its 5-methyl form (5-methyltetrahydrofolate) are major active forms in vivo,
co-enzymes in the metabolism of one-carbon units, the production of nucleotides, nucleic acids, and the metabolism of haem.

119
Q

vitamin B9/folic acid deficiency

A

Folic acid deficiency is most commonly associated with complications in pregnancy – babies are more likely to be premature, with low birth weight and an increased risk of neural tube defects, such as spina bifida.
Recommended that folic acid is taken while attempting to get pregnant until 12 weeks pregnant.

120
Q

How is vitamin B12/cobalamin synthesised and where is it sourced from?

A

Synthesised by bacteria, meaning there is little to be found in dietary plants. Liver, meat, eggs and milk are good sources

121
Q

what is vitamin B12/cobalamin a co-enzyme for?

A

Cobalamin is a co-enzyme responsible for metabolism of one-carbon units, DNA synthesis and formation of red blood cells.

122
Q

What condition may make your body be unable to absorb vitamin B12?

A

When ingested, vitamin B12 combines with a protein in the stomach called “intrinsic factor”.
This mix of vitamin B12 and intrinsic factor is then absorbed in the distal ileum.
Pernicious anaemia causes your immune system to attack the cells in your stomach that produce intrinsic factor, which makes your body unable to absorb vitamin B12.

123
Q

What does vitamin C activity refer to?

A

both ascorbic acid and its oxidised form dehydro-ascorbic acid (DHAA)

124
Q

Sources of ascorbic acid

A

Fruits and vegetables are the best source of ascorbic acid.
However, the major source of vitamin C in the British diet is the potato

125
Q

What is ascorbic acid and what is it necessary for

A

Known as antioxidant
But is an enzymatic co-factor for hydroxylation reactions, and thus necessary for the formation of collagen (cartilage, scar tissue, blood vessels) and the production of noradrenaline from dopamine.
Ascorbic acid also enhances the uptake of dietary non-haem iron

126
Q

Enzymatic co factor

A

a molecule that increases the rate of reaction or is required for enzyme function

127
Q

Deficiency of ascorbic acid/vitamin C and symptoms

A

responsible for scurvy, whereby insufficient cross linking of collagen results in slow healing of wounds, bleeding gums and mucous membranes, tooth loss, pale skin and nervous dysfunction.

128
Q

What is considered the major active form of vitamin A

A

Retinol

129
Q

sources of retinol/vitamin A

A

. Butter, cheese and cod liver oil are good sources

130
Q

How is vitamin A derived from animal tissue absorbed?

A

Vitamin A derived from animal tissues has a high degree of bioavailability and is rapidly absorbed.
Retinyl esters of long chain fatty acids are hydrolysed then re-esterified by intestinal mucosa during absorption, then bound by retinol-binding protein in the liver.
This form can be released from the liver as needed, and subsequently hydrolysed to retinol.

131
Q

How is vitamin A derived from plant sources absorbed?

A

absorbed after the conversion of carotenoids (yellow/orange pigments) to retinol in the small intestine.
Conversion to retinol is adaptive and inversely related to β-carotene intake, meaning the risk of vitamin A toxicity from consuming plant sources is low

132
Q

What Is vitamin A used for?

A

is used to produce rhodopsin
also plays a role in bone metabolism, whilst retinoic acid is necessary for gene transcription, reproduction and skin health.
carotenoids and vitamin A also have antioxidant activity.

133
Q

signs of vitamin A deficiency

A

night blindness and skin legions. Acute cases can lead to abnormal bone development, reproductive disorders and death.

134
Q

What does vitamin D occur in the diet as

A

cholecalciferol

135
Q

how can vitamin D be made and where can it be found

A

Made in the skin in sunlight through the conversion of an intermediate in the cholesterol cycle
Cholecalciferol can be found in dairy products and egg yolk but oily fish is the best source

136
Q

How is cholecalciferol absorbed

A

Cholecalciferol is converted in the liver to calcifediol which is converted to calcitriol (the active form of vitamin D) in the kidneys.
Calcitriol increases blood levels of calcium by increasing its uptake in the intestine (along with its phosphate counterion), and through increased resorption of bone mineral.

137
Q

deficiency of vitamin D

A

Deficiency can result in rickets, which causes bones to become soft and weak, which can lead to bone deformities

138
Q

What is vitamin E responsible for

A

potent antioxidant, responsible for protecting lipids in cell membranes from oxidative damage

139
Q

deficiency in vitamin E

A

Due to their role carrying oxygen around the body, red blood cells are at particular risk of oxidation in vitamin E-deficient patients.

140
Q

what does vitamin K activity refer to

A

a group of compounds containing an active naphthoquinone ring

141
Q

where are vitamin K1 found

A

Vitamin K1 is phylloquinone produced during photosynthesis and is therefore found at highest levels in leafy green vegetables

141
Q

where is vitamin K2 found

A

The vitamin K2 group are the menaquinones. Whilst K2 compounds are found in meat, eggs and dairy products, our own gut bacteria also produce them.

142
Q

what is vitamin K essential for

A

blood clotting/coagulation as it is a co-factor for a liver enzyme required to carboxylate glutamate residues to make them fully functional

143
Q

deficiency in vitamine k

A

leads to bleeding disorders

144
Q

what is warfarin used for and how does it work

A

which is given to reduce risk of coagulation in patients at risk of developing clots
works by binding vitamin K epoxide reductase, the enzyme that recycles oxidized vitamin K1 to its active reduced form

145
Q

co factors

A

separate (non-protein) molecules or ions that must bind with an enzyme to make it work, either by joining with the active site directly, or by stimulating a conformational change to the protein that (in turn) changes the shape of the active site
can be referred to as co enzymes

146
Q

drug

A

a foreign compound taken into an organism that changes the behaviour of a biological process for therapeutic benefit

147
Q

what was lipinskis general observation

A

that most medicinal drugs were relatively small, lipophilic molecules

148
Q

lipinskis rule of five

A

says that a molecule of an orally active drug usually obeys at least three of the following criteria:

  • Not more than 5 hydrogen bond donors, e.g., an alcohol group, -OH, or an amine group (primary, -NH2, or secondary, -NHR);
  • Not more than 10 hydrogen bond acceptors, nitrogen atoms, N, or oxygen atoms, O;
  • A relative molecular mass of less than 500;
  • An octanol-water partition coefficient logP not greater than 5.
149
Q

receptor

A

the specific chemical constituents of the cell with which a drug interacts to produce its pharmacological effects

150
Q

how does cisplatin work

A

A platinum-based anticancer drug, exerts its therapeutic effect by platinating the N-7 position of guanine on the major groove site of the DNA double helix (Figure 34). This chemical modification of the platinum atom crosslinks two adjacent guanines on the same DNA strand. This blocks replication and inhibits transcription, resulting in DNA damage and subsequently cell death.

151
Q

Example of ionic bonds in drugs

A

interaction between the protonated amino group on salbutamol (inhaler to relieve asthma and breathlessness) and the dissociated carboxylic acid group of its receptor site .

MPharm Stage 1 (14 decks)

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