RESUMEN
Aim: E-selectin is overexpressed on angiogenic and inflamed endothelium. Molecules binding to E-selectin with high affinity and specificity enable its use as a molecular imaging biomarker. Material & methods: The interactions of four different peptides (i.e., Ac-P1 [Acetyl-IELLQAR-CONH2], H2N-P2 [H2N-DITWDQLWDLMK-CONH2], H2N-P3A5 [H2N-YRNWAGRW-CONH2], and Ac-P4 [Acetyl-YRNWDGRW-CONH2]) with E-selectin were analyzed by computational methodologies, surface plasmon resonance and in vitro using activated human umbilical vein endothelial cells. Poly(butyl cyanoacrylate) microbubbles were functionalized with the best candidates and evaluated as molecular ultrasound probes in cultured cells and explanted carotid arteries. Results: H2N-P3A5 and Ac-P4 peptides bound stronger to E-selectin than Ac-P1 and H2N-P2, but with lower specificity. H2N-P2 bound with higher specificity and affinity than Ac-P1. Conclusion: H2N-P2 is a good candidate for designing E-selectin-targeted molecular imaging agents.