Oxime formation between carbonyls in biological species and aminooxy groups in metal chelates

Interplay of biological molecules is of vital importance for the life of biological entities encompassing a whole world of biological interactions where myriads of binding events take place every second. The nature of interactions determines the biological function whether it is transmission, signaling, catalysis, movement, assembly or sensing. The interactions involve all types of binding from van der Waals interactions to strong covalent bonds. Protein-protein interactions information allows the function of a protein to be defined by its position in a complex web of interacting proteins. Access to such information will aid biological research and potentially make the discovery of drug targets much easier.;For these reasons, this dissertation focuses to study the protein-protein interactions between CD20 antigen and IgG antibody, using 1F5 as a model. The use of a new artificial proteases AOE-Fe(III) that is able to cleavage membrane proteins on the surface of B cells when it is conjugated with 1F5 through an oxime bond.;Then, the description of a new way to purify proteins using the 6His and NTA-Ni, between a protein that has an aldehyde group made by mutagenesis (Aldehyde-MBP) with a metal-chelate (derivative of NTA) that is able to capture nickel ions through an oxime bond or Schiff base.