Cross-linked protein matrices were constructed using fibrinogen and albumin with ethyl-dimethyl-aminopropylcarbodiimide (EDC) and N-hydroxy-succinimide (NHS) on silicon plates.  EDC/NHS forms an amine reactive carboxyl intermediate, and amine bonds between proteins can thereby be formed. The plates with protein matrices were exposed to 0.1mg/ml solutions of risedronate, gamma tocotrienol, and interferon gamma for an hour of incubation.  The addition of protein and drug layers was determined by null ellipsometry and the structural integrity of the protein matrices were tested with a 0.1% w/w detergent of sodium dodecyl sulfate (SDS).  The results demonstrate that risdronate, gamma-tocotrienol and interferon-gamma actively bind to the surface of cross-linked layers of albumin without the assistance of the EDC/NHS catalyst on top.  However, only gamma-tocotrienol will actively bind to the surface of cross-linked layers of fibrinogen and inteferon-gamma will only bind to fibrinogen surfaces that are activated with EDC/NHS.  The data shows albumin is an efficient drug carrier that is capable of transporting various types of drugs, not only through the body but also after immobilization to surfaces.