抄録
The number of therapeutic antibody under development has increased markedly over the last several years and this trend continues. In fact, there are more than 20 approved antibodies on the US market. One of the most important characteristics of the antibodies for the successful development as biotherapeutics is their conformational stability, which can be defined as the ability of molecule to maintain the native higher-order structure under broad range of conditions. The antibodies in unfolded state frequently have greater propensity to form aggregates than those in native state. The differential scanning calorimetry (DSC) is the only technique for direct measurement of the thermodynamic parameters accompanied by the thermal unfolding. The DSC is also an effective tool to estimate the contribution of each domain to overall stability for multi-domain protein such as antibodies. Although thermal stabilities of different antibodies have been examined by using DSC, apparent unfolding temperature where heat capacity takes maximum value was mainly discussed and thermodynamic parameters of each domain and inter-domain interactions were not estimated. It is now expected to establish analytical technique that takes intrinsic stabilities of each domain and inter-domain interactions into account for complete understanding of thermodynamics of whole antibody.
https://ror.org/027y26122 
