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A solution for Allosterity and Cooperativity

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1. Explain in your own words why increasing the hydrophobicity of a drug leads to "entropic optimization" of the binding affinity. Please consider all of the entropic changes that occur in drug binding and how they alter affinity.
2. What are the limitations of this approach to affinity optimization?
3. Please identify some other examples of the practical application of the entropy/enthalpy compensation principle.

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Solution Summary

The solubility of drug molecules contributes to their affinity to bind to protein receptor sites of action.
This solution explains the relation between entropy optimization, hydrophobicity and entropy and provides practical examples of the use of this principle in drugs that are available in the market.
The student is invited to reead further on the references proposed.

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A solution for Allosterity and Cooperativity

When a compound made up of non-polar molecules is mixed with an aqueous solvent such as water, the molecules cluster together into a ball while water tends to form a ring around them. They do so because they are hydrophobic (. Wikibooks 2015).
When more of this solute is added, the water ring is disturbed as more of the hydrophobic molecules join the non-polar core and the displaced water molecules are freed to move around. This causes high disorder in the solution environment referred to as high entropy.
According to the 2nd Law of Thermodynamics, "The total entropy of the system plus its surrounding must always be ...

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