Ricerc@Sapienza

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 avb3 and avb5 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 avb5. 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.