AFFINITY OF ANTIFLUORESCEIN ANTIBODIES ENCAPSULATED WITHIN A TRANSPARENT SOL-GEL GLASS

Low temperature processed, porous sol-gel glasses represent a new clas s of materials for immobilization of biomolecules. The ability to form these materials into films, monoliths, and fibers to produce high-pur ity, porous glasses and the fact that they are optically transparent a nd chemically inert make them an intriguing platform for the developme nt of chemical biosensors. In this paper, we report on the first attem pt to encapsulate an intact antibody in a sol-gel glass matrix. Specif ically, we present results on the affinity of sol-gel-encapsulated pol yclonal antifluorescein. The results demonstrate that the sol-gel-enca psulated antibody retains an affinity for fluorescein; the affinity co nstant (K(f)) for antibody-hapten complex is on the order of 107 M-1. The encapsulation process decreases K(f) by about 2 orders of magnitud e compared to the native system in buffer solution. The effect of agin g and drying on the K(f) for sol-gel-encapsulated antifluorescein is r eported. Finally, we demonstrate that the intact antibody affinity can be maintained using simple storage protocols.