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ANTIBODY AFFINITY:
 Affinity measures the strength of interaction between an epitope
and an antibodys antigen binding site
 It is the sum of the attractive and repulsive forces between them
 Affinity is the equilibrium constant that describes the antigen
antibody reaction
 Antibody affinity is measured as Ka
KA = affinity constant
[Ab] = molar concentration of unoccupied binding sites
on the antibody
[Ag] = molar concentration of unoccupied binding sites
on the antigen
[Ab-Ag] = molar concentration of the antibody-antigen
complex
 A low affinity antibody binds the concerned antigen weakly
and it tends to dissociates readily
 A high affinity antibody binds the concerned antigen more
tightly and tends to reamin longer
ANTIBODY AVIDITY:
 Avidity gives a measure of the overall strength of an antibody-
antigen complex.
 It is dependent on three major parameters:
 Affinity of the antibody for the epitope
 Valency of both the antibody and antigen
 Structural arrangement of the parts that interact
 All antibodies are multivalent e.g. IgGs are bivalent and
and IgMs are decavalent.
 The greater an immunoglobulin’svalency (number of antigen
binding sites), the greater the amount of antigen it can bind.
 Similarly, antigens can demonstrate multivalency because they
can bind to more than one antibody.
 Multimeric interactions between an antibody and an antigen
help their stabilization.
 High avidity can compensate for low affinity
PentamericIgM has a lower affinity than IgG but has a higher avidity
than IgG due to its multivalence

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Antibody affinity and avidity

  • 1. ANTIBODY AFFINITY:  Affinity measures the strength of interaction between an epitope and an antibodys antigen binding site  It is the sum of the attractive and repulsive forces between them  Affinity is the equilibrium constant that describes the antigen antibody reaction  Antibody affinity is measured as Ka KA = affinity constant [Ab] = molar concentration of unoccupied binding sites on the antibody [Ag] = molar concentration of unoccupied binding sites on the antigen [Ab-Ag] = molar concentration of the antibody-antigen complex  A low affinity antibody binds the concerned antigen weakly and it tends to dissociates readily  A high affinity antibody binds the concerned antigen more tightly and tends to reamin longer ANTIBODY AVIDITY:  Avidity gives a measure of the overall strength of an antibody- antigen complex.  It is dependent on three major parameters:
  • 2.  Affinity of the antibody for the epitope  Valency of both the antibody and antigen  Structural arrangement of the parts that interact  All antibodies are multivalent e.g. IgGs are bivalent and and IgMs are decavalent.  The greater an immunoglobulin’svalency (number of antigen binding sites), the greater the amount of antigen it can bind.  Similarly, antigens can demonstrate multivalency because they can bind to more than one antibody.  Multimeric interactions between an antibody and an antigen help their stabilization.  High avidity can compensate for low affinity PentamericIgM has a lower affinity than IgG but has a higher avidity than IgG due to its multivalence