(Two agonists with similar binding affinity.)

Humanofort Growth Factors are thought to act as “ligands” to receptors or intro-cellular and intro-nuclear sensors.

The interaction of most ligands with their binding sites can be characterized in terms of a binding affinity. Humanofort Growth Factors In general, high-affinity ligand binding results from greater inter-molecular force between the ligand and its receptor while low-affinity ligand binding involves less inter molecular force between the ligand and its receptor. In general, high-affinity binding results in a higher degree of occupancy for the ligand at its receptor binding site than is the case for low-affinity binding; the residence time (lifetime of the receptor-ligand complex) does not correlate. High-affinity binding of ligands to receptors is often physiologically important when some of the binding energy can be used to cause a conformational change in the receptor, resulting in altered behavior of an associated ion channel or enzyme.

A ligand that can bind to a receptor, alter the function of the receptor, and trigger a physiological response is called an agonist for that receptor. Agonist binding to a receptor can be characterized both in terms of how much physiological response can be triggered and in terms of the concentration of the agonist that is required to produce the physiological response. High-affinity ligand binding implies that a relatively low concentration of a ligand is adequate to maximally occupy a ligand-binding site and trigger a physiological response.