A selective α v β 5 integrin antagonist hidden into the anophelin family protein cE5 from the malaria vector Anopheles gambiae

A RGD motif was identified in the N‐terminal region of cE5, a potent salivary thrombin inhibitor from the African malaria vector Anopheles gambiae . A peptide (APQ30) encompassing the first 30 amino acids residues of the protein and including the RGD tripeptide was tested in cell adhesion assays and found to inhibit α v β 3 and α v β 5 mediated adhesion. A shorter peptide (APQ16), strongly conserved among members of the A. gambiae species complex and including only the first 16 residues, retained adhesion inhibitory properties, however with enhanced specificity toward α v β 5 . In addition, migration and invasion assays showed its capacity to inhibit the invasiveness of the malignant cell lines HepG2 and MDA‐MB231. Altogether our data point to APQ16 as a new promising candidate as theranostic agent.