Representation of affinity in the case of co-operativity in protein-ligand binding.
We have already proposed a "Global Association Function" to represent the global affinity of proteins to a drug; it was first applied in the case of independent binding sites. In this paper, we show that this same function can also be used to assess interactions between sites by varying the number of interacting sites and their co-operativity level. The resulting curves in two application cases are given together with the corresponding Scatchard plot: i) in a system with one single class of identical and interacting sites, ii) in a system with two classes of sites in which either primary or secondary are interacting; unexpectedly, in this latter case we also observed that sometimes positive co-operativity occasionally resulted in a concave-up Scatchard plot which is unusually admitted. In addition, as described in one example, our function is assumption free; this might be an advantage over usual methods, such as discrete parameter methods, because they require additional and empirical hypotheses on their related binding model.
Monot
C
C
CNRS, URA 1288, Faculté de Médecine, Vandoeuvre-Les-Nancy, France.
Lapicque
F
F
Benamghar
L
L
Muller
N
N
Payan
E
E
Netter
P
P
D001665:Binding Sites; D006801:Humans; D008024:Ligands; D008954:Models, Biological; D011485:Protein Binding
D008024:Ligands