Abstract
Recently, following with the development of biotechnology, active core peptides of many bioactive proteins were identified and these bioactive peptides have been shown to be potential candidates for therapeutic agents. But their clinical application have been limited because of their low in vivo stability caused by enzymatic degradation and rapid renal excretion from blood. To enhance the therapeutic usefulness of bioactive peptide, a polymeric modifier, SMA (poly(styrene co-maleic anhydride)) which is known as binding to plasma albumin, was applied to conjugate a synthetic cell-adhesive laminin-derived peptide YIGSR, and their inhibitory effect on lung metastasis of B16BL6 melanoma cells were examined. SMA conjugated YIGSR (SMA-YIGSR) showed a marked antimetastatic effect than native peptide YIGSR in terms of molar ratio of YIGSR. In addition, SMA-YIGSR was found to bind efficiently to albumin by affinity chromatography but not YIGSR. So it is assumed that the binding to plasma albumin might result in a longer plasma half-life. In order to make the mechanism of enhancement of antimetastatic effect more clearly, now pharmacokinetics of SMA-YIGSR and binding affinity of SMA-YIGSR to albumin were on study.
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