Question:
What is the effect of stereochemistry on Drug-Receptor interactions?
What is the effect of stereochemistry on Drug-Receptor interactions?
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A receptor is like a lock and a drug is like a key. The binding pocket of a receptor is three-dimensional and is itself chiral (it is built from chiral amino acids). So the shape of the drug matters a lot.
Updated On: Jun 24, 2026
- Both enantiomers fit equally well into a receptor site
- Only one isomer may fit in the chiral binding site of the receptor
- Geometric isomers always have the same activity
- Chirality does not influence receptor binding
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The Correct Option is B
Solution and Explanation
Concept:
A receptor is like a lock and a drug is like a key. The binding pocket of a receptor is three-dimensional and is itself chiral (it is built from chiral amino acids). So the shape of the drug matters a lot.
Why stereochemistry matters:
Many drugs have a chiral centre, which means they can exist as two mirror-image forms called enantiomers. These two forms are not the same shape in 3D, just like your left and right hand. Only one of them usually fits neatly into the receptor's binding site.
Step 1:
Because the binding site has a fixed 3D shape, one enantiomer can slot in and make good contacts, while the other one does not fit well and shows little or no activity.
Step 2:
So it is wrong to say both enantiomers fit equally (Option 1), or that geometric isomers always behave the same (Option 3), or that chirality has no effect (Option 4). All of these ignore the real 3D matching that happens.
Answer: Option (2) — Only one isomer may fit in the chiral binding site of the receptor.
A receptor is like a lock and a drug is like a key. The binding pocket of a receptor is three-dimensional and is itself chiral (it is built from chiral amino acids). So the shape of the drug matters a lot.
Why stereochemistry matters:
Many drugs have a chiral centre, which means they can exist as two mirror-image forms called enantiomers. These two forms are not the same shape in 3D, just like your left and right hand. Only one of them usually fits neatly into the receptor's binding site.
Step 1:
Because the binding site has a fixed 3D shape, one enantiomer can slot in and make good contacts, while the other one does not fit well and shows little or no activity.
Step 2:
So it is wrong to say both enantiomers fit equally (Option 1), or that geometric isomers always behave the same (Option 3), or that chirality has no effect (Option 4). All of these ignore the real 3D matching that happens.
Answer: Option (2) — Only one isomer may fit in the chiral binding site of the receptor.
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