Properties of mitomycin C-albumin conjugates in vitro and in vivo

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Abstract
Mitomycin C, an antineoplastic agent, was covalently attached to bovine serum albumin through a spacer of the glutaryl group. Two different synthetic methods were adopted; one was by the prior glutarylation of albumin followed by binding to mitomycin C, and the other was by the synthesis of glutarylated mitomycin C followed by binding to albumin. Physicochemical properties of the conjugates, such as Stokes radius, molecular weight, and helical content, were comparatively examined. The glutarylation of albumin resulted in an increase in Stokes radius of the protein due to the conformational change. The conjugates significantly stabilized mitomycin C and liberated it gradually under the physiological condition (t1/2 = 66-84 h). Both conjugates accumulated effectively in the tumor tissues. However, the distribution behavior of the conjugates depended on physicochemical properties such as molecular size. Treatment with the conjugates suppressed the tumor growth and increased the survival rate in the tumor-bearing mice.

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