TRANSPORT OF HYDROPHOBIZED FRAGMENTS OF ANTIBODIES THROUGH THE BLOOD-BRAIN-BARRIER

HYDROPHOBIZED and non-hydrophobized Fab fragments of human antibodies against gliofibrillar acid protein (GFAP) and brain specific alpha(2)- glycoprotein (alpha(2)GP) were used to study their penetration through the blood-brain barrier (BBB). These Fab fragments were modified by s tearoyl chloride in reversed micelles of aerosol OT in octane (one or two fatty acid residues attached to protein molecule). Modified and no n-modified I-125-labelled Fab fragments were intracardially administer ed to rats. The amount of label accumulated in brain was 55% higher th an the total amount in all other organs. In contrast, non-hydrophobize d Fab fragments did not penetrate through the BBB. We assume that the artificial hydrophobization of Fab fragments can increase their capabi lity to penetrate through the cell membranes and, in particular, the B BB.