Self-Assembling CAV-C Peptide Nanostructures as Antagonists of CXCR4-Mediated Migration in HCC
Alejandro Ruperti-Repilado – PhD Student, Chemistry in Pharmaceuticals Sciences, Universidad Complutense de Madrid (UCM); Mohammed Alqudwa Fattouh – PhD Student, Chemistry in Pharmaceuticals Sciences, Universidad Complutense de Madrid (UCM); Juan Pedro Cascales-Sandoval – Associate Researcher, Chemistry in Pharmaceuticals Sciences, Universidad Complutense de Madrid (UCM); Jorge Rubio-Retama – Full Professor, Chemistry in Pharmaceuticals Sciences, Universidad Complutense de Madrid (UCM)
Associate Professor Universidad Complutense de Madrid (UCM) Madrid, Madrid, Spain
Introduction: Caveolin-1 (CAV-1) is a membrane-associated protein involved in proliferation, apoptosis, and signal transduction, with context-dependent roles in cancer. In hepatocellular carcinoma, the Caveolin-1 scaffolding domain (CSD) stabilizes CXCR4, enhancing CXCL12-mediated signaling and promoting migration and invasion. We developed a peptide nanoparticle system based on a CSD-derived hydrophobic subunit (CAV-C) combined with a hydrophilic sequence, enabling amphiphilic self-assembly into nanospheres. Acting as a CXCR4 antagonist, CAV-C nanospheres disrupt the CXCR4-CXCL12 interaction and significantly reduce HepG2 cell migration and invasion.
Learning Objectives:
understand the structurally designed synthesis and self-assembly processes of the peptide-based nanospheres.
realise the anti-migratory and anti-invasive effects driven by CXCR4 antagonism by the proposed nanosystem.
