Antigen binding thermodynamics and antiproliferative effects of chimeric and humanized anti-p185HER2 antibody fab fragments

A study was conducted on murine monoclonal and humanized anti-p185HER2 antibody fab fragments in order to determine their antigen binding and antiproliferative effects. Results showed a correct folding of the Escherichia coli produced fab. The observed enthalpy changes differed and indicated differences in the antigen binding mechanisms. Results further suggested that KD measurements were not fully efficient in reproducing humanized murine antibody activity. Thermionic data also revealed information on the hydrophobic and vibrational contributions to binding.