SURFACE MODIFICATION OF ALBUMIN MICROSPHERES

Submicron sized hydrophobic and hydrophilic albumin microspheres (MS) were prepared using a chemical crosslinking technique. Spermine was li nked to the surface of the hydrophilic MS. The degree of hydrophobicit y for these three types of MS was investigated using a novel technique of sedimentation volume. The surface tension of the hydrophobic MS wa s 31 mN m(-1). The ST of the hydrophilic MS was 68 mN m(-1), whereas t he surface tension of spermine-linked MS corresponded to 62, 65.5, 69 and 71 mN m(-1) indicating heterogeneous hydrophilic characteristics. Ligands can be successfully linked to MS using a water-soluble carbodi imide.