Determining the pharmacophore of a group of isosteres

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In summary, KI is the binding constant for an inhibitor in biochemistry. It is the equilibrium dissociation constant for the binding reaction between an inhibitor and an enzyme. A lower KI value indicates a more potent inhibitor.
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mycotheology
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Heres the question:
http://img442.imageshack.us/img442/484/sarr.png
Firstly does anyone know what Ki is? Ionisation constant? I'm guessing its proportional to the drugs potency. I could take a good guess by observing the differences between each isostere but I'm guessing there's some kind of method I should be able to use here.
 
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In biochemistry, KI is the binding constant for an inhibitor. Put more precisely, in the binding interaction between an inhibitor I and enzyme E, which form enzyme-inhibitor complex EI:

E + I <--> EI

KI is the equilibrium dissociation constant for the binding reaction:

[tex]K_I = \frac{[E]}{[EI]}[/tex]

Therefore, more potent inhibitor have lower KI values.
 

FAQ: Determining the pharmacophore of a group of isosteres

What is a pharmacophore?

A pharmacophore is a hypothetical 3D arrangement of chemical features that are necessary for a molecule to interact with a specific biological target and elicit a particular biological response.

What are isosteres?

Isosteres are molecules or groups of atoms that have similar shapes and sizes and similar chemical and physical properties, but different chemical structures.

Why is it important to determine the pharmacophore of a group of isosteres?

Determining the pharmacophore of a group of isosteres can help identify the key structural and functional features that are responsible for the biological activity of the molecules. This information can be used to design new drugs with improved potency, selectivity, and reduced side effects.

How is the pharmacophore of a group of isosteres determined?

The pharmacophore of a group of isosteres is typically determined using computational methods, such as molecular docking and pharmacophore modeling. These methods involve analyzing the interactions between the isosteres and the target protein, and identifying common structural features that are necessary for binding and activity.

Can the pharmacophore of a group of isosteres change with different target proteins?

Yes, the pharmacophore of a group of isosteres can vary depending on the target protein. This is because different proteins may have different binding sites and require different structural features for optimal binding and activity. Therefore, it is important to determine the pharmacophore for each specific target protein.

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