Fig. 1. The Seahorse-peptide with amino acid sequence similarity to α-enolase decreases the interaction of α-enolase and plasminogen. (A) A strong sequence similarity (92%) between human α-enolase (amino acids 293-304) and seahorse-derived peptide. All sequences were obtained from GenBank protein sequence data with accession numbers: Human (NP 001419), E. coli (AAC69289), S. pnuemoniae (AAC17130), and T. brucei (AAF73201). (B) Specific binding of plasminogen to α-enolase. Plasminogen binds to α-enolase immobilized on microtiter well plates in a concentration-dependent manner. ELISA was performed in a multiwall plate coated with α-enolase (1 μg/well) and increasing amounts of human plasminogen (1-5 μg). Control wells lacked α-enolase and were coated with only BSA (1 μg/well). The results represent the average from three independent experiments. (C) Inhibitory effect of seahorsepeptide on the interaction between α-enolase and plasminogen. Various concentration of seahorse peptide were added to wells containing 1 μg immobilized α-enolase, followed by the addition of 2 μg plasminogen, and ELISA was performed as described in Materials and Methods. The results represent the average from three independent experiments. *P ＜ 0.05 compared with controls.