ISSN:
1572-8943
Keywords:
anti-idiotypic antibody cascade
;
Human Melanoma-Associated-Antigen (HMW-MMA)
;
protein-protein binding
;
thermodynamic
;
titration calorimetry
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract An uptake or a release of heat accompanies practically all molecular binding interactions. Therefore isothermal titration microcalorimetry is universally applicable for the characterisation of such binding processes. Calorimetric analyses do not require marker molecules or intrinsic spectroscopic reporter groups, which can modify the analysed interactions. Furthermore, measurements are carried out in solution and the adsorption of reactants to a solid phase is thus avoided. At variance with most other analytical approaches, titration calorimetry determines simultaneously enthalpy and entropy contributions of the binding interactions, as well as the binding constant and stoichiometry. In our analyses of the interactions between monoclonal antibodies and candidate antigens for vaccines vs. malaria and malignant melanoma, isothermal titration calorimetry has turned out to be a very valuable technique. The obtained quantitative data on biomolecular interactions can substantially support the rational design of epitope-focused vaccines.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1010162429900
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