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A selective α v β 5 integrin antagonist hidden into the anophelin family protein cE5 from the malaria vector Anopheles gambiae
Author(s) -
Di Gaetano Sonia,
Del Gatto Annarita,
Pirone Luciano,
Comegna Daniela,
Zaccaro Laura,
Saviano Michele,
Arcà Bruno,
Capasso Domenica,
Pedone Emilia
Publication year - 2018
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.533
H-Index - 7
ISSN - 2475-8817
DOI - 10.1002/pep2.24054
Subject(s) - anopheles gambiae , tripeptide , peptide , malaria , integrin , biology , vector (molecular biology) , cell adhesion , microbiology and biotechnology , biochemistry , cell , immunology , recombinant dna , gene
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.