Chemical biology aimed at the development of new thrombolytics

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Structure-activity relationships of cyclic pentapeptide, malformin A1 (MA1), showed that the formation of intramolecular disulfide bond and the existence of hydrophobic side-chains were essential for the enhancement of fibrinolysis by MA1. In addition, the correlation between enhancement of fibrinolysis and cytotoxicity was not observed, suggesting that the separation of each activity is possible. The studies using radioisotope-labeling and fluorescence-labeling revealed the intracellular localization of MA1. Moreover, malformin-affinity beads detected 65 kDa and 22 kDa cellular malformin-high affinity proteins.