Department of Pharmacy AY2021-2022. PHA213 Learning lab guide –
Semester 1
Learning lab 1: Introduction to Chemistry of Drug Action (2%)
Answer the following questions:
1. A hypothetical compound (I) isolated from a marine sponge was found to exhibit
promising blood pressure-lowering activity by virtue of its ability to inhibit a
specific enzyme in the body. Compounds II, III and IV were made as analogues
and tested for their binding affinity. Compounds II and III were found to exhibit
reduced affinity for the enzyme, whilst compound IV bound the enzyme much
more strongly. Provide a possible explanation for these results.
First compound “2” has a big difference comparing to compound 1, were coo- group
are absent which reduces the affinity comparing to compound 1, and compound 3 has
coo- group but far away from HO which will not having an interaction between both
group so affinity is also not high, but at compound 4 we can see that the coo- group
close enough to make an interaction between the HO and COO- which that will cause a
hydrogen bounding to result a high affinity comparing to other compound showing.
2. Glutamate receptors are transmembrane receptors located on neuron
membranes. These receptors bind the neurotransmitter L-glutamate. Numerous
compounds have been designed that block glutamate from binding to these
receptors and activating them. Two examples of such “antagonists” are shown
below. One of these acts as a normal antagonist, whilst the other acts as an
allosteric antagonist. Which do you think is which, and why?
AP-7 are the antagonists because its similar compound to the L-glutamate which can
approximately identical binding region in enzyme, and YM-202074 are the allosteric inhibition
because of the complete different molecule
1
, Department of Pharmacy AY2021-2022. PHA213 Learning lab guide –
Semester 1
3. The hormone adrenaline interacts with proteins located on the surface of cells
and does not cross the cell membrane. However, large steroid molecules such
as oestrone cross cell membranes and interact with proteins located in the cell
nucleus. Why is a large steroid molecule like oestrone able to cross the cell
membrane when a smaller molecule such as adrenaline cannot?
Oestrone is more hydrophobic because of carbons and less functional groups so
dissolve through fatty membrane because of the hydrophobic character, were the
adrenaline has more functional groups with less carbons which make it polar.
2
Semester 1
Learning lab 1: Introduction to Chemistry of Drug Action (2%)
Answer the following questions:
1. A hypothetical compound (I) isolated from a marine sponge was found to exhibit
promising blood pressure-lowering activity by virtue of its ability to inhibit a
specific enzyme in the body. Compounds II, III and IV were made as analogues
and tested for their binding affinity. Compounds II and III were found to exhibit
reduced affinity for the enzyme, whilst compound IV bound the enzyme much
more strongly. Provide a possible explanation for these results.
First compound “2” has a big difference comparing to compound 1, were coo- group
are absent which reduces the affinity comparing to compound 1, and compound 3 has
coo- group but far away from HO which will not having an interaction between both
group so affinity is also not high, but at compound 4 we can see that the coo- group
close enough to make an interaction between the HO and COO- which that will cause a
hydrogen bounding to result a high affinity comparing to other compound showing.
2. Glutamate receptors are transmembrane receptors located on neuron
membranes. These receptors bind the neurotransmitter L-glutamate. Numerous
compounds have been designed that block glutamate from binding to these
receptors and activating them. Two examples of such “antagonists” are shown
below. One of these acts as a normal antagonist, whilst the other acts as an
allosteric antagonist. Which do you think is which, and why?
AP-7 are the antagonists because its similar compound to the L-glutamate which can
approximately identical binding region in enzyme, and YM-202074 are the allosteric inhibition
because of the complete different molecule
1
, Department of Pharmacy AY2021-2022. PHA213 Learning lab guide –
Semester 1
3. The hormone adrenaline interacts with proteins located on the surface of cells
and does not cross the cell membrane. However, large steroid molecules such
as oestrone cross cell membranes and interact with proteins located in the cell
nucleus. Why is a large steroid molecule like oestrone able to cross the cell
membrane when a smaller molecule such as adrenaline cannot?
Oestrone is more hydrophobic because of carbons and less functional groups so
dissolve through fatty membrane because of the hydrophobic character, were the
adrenaline has more functional groups with less carbons which make it polar.
2
