The influence of rigid or flexible linkage between two ligands on the effective affinity and avidity for reversible interactions with bivalent receptors.
Bivalent or polyvalent cooperative binding between ligand and receptor is much tighter and more efficient than monovalent binding of the same counterparts. Because of this, many biological processes involve polyvalent binding for realization of regulatory mechanisms. For this reason it is necessary to develop a general formalism for prediction of the relationship between the binding affinities of each ligand subunits, the length of the flexible linker between them and avidity of the interaction. Here, we consider an approach that is based on the description of the state of equilibrium for the reaction of mono- and multivalent ligand-receptor binding of algebraic equation systems. This approach allows the evaluation of the avidity of bivalent binding and to determine the concentrations of ligand-receptor complexes, which will be obtained at the equilibrium state. The analysis presented here may be useful in analysing the binding behaviour of a bivalent receptor and a ligand consisting of two subunits covalently connected with a rigid or flexible linker.
Bobrovnik
S A
SA
Department of Molecular Immunology, Palladin Institute of Biochemistry, Kiev 01601, Ukraine. sab@biochem.kiev.ua
D001665:Binding Sites; D008024:Ligands; D008954:Models, Biological; D008962:Models, Theoretical; D016254:Mutagenesis, Insertional / Q000502:physiology; D011485:Protein Binding; D021122:Protein Subunits / Q000737:chemistry; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D008024:Ligands; D021122:Protein Subunits; D011956:Receptors, Cell Surface; D011994:Recombinant Proteins