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Deciphering RGDechi peptide‐α 5 β 1 integrin interaction mode in isolated cell membranes
Author(s) -
Russo Luigi,
Farina Biancamaria,
Del Gatto Annarita,
Comegna Daniela,
Di Gaetano Sonia,
Capasso Domenica,
Liguoro Annamaria,
Malgieri Gaetano,
Saviano Michele,
Fattorusso Roberto,
Zaccaro Laura
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/pep2.24065
Subject(s) - integrin , peptide , computational biology , microbiology and biotechnology , receptor , chemistry , biophysics , biology , biochemistry
Integrins are a large family of heterodimeric receptors critically engaged in pathological processes such as tumor progression and metastasis. Although they are validated therapeutic targets, the molecular determinants governing integrin‐ligand interactions are not yet fully understood, leading to a scarcity of integrin sub‐type exclusive antagonists. In the past decade, we have investigated the biological behavior of the RGDechi, a chimeric peptide able to specifically bind α v β 3 integrin without cross reacting with α v β 5 and α IIb β 3 integrins. Here we have investigated the capability of the peptide to bind α 5 β 1 integrin and characterized the molecular determinants governing this interaction through a combined experimental and computational approach. The detailed comparison of RGDechi‐α 5 β 1 structural model with that previously determined of RGDechi in complex with α v β 3 shows how the bifunctional nature of the peptide renders the molecule an important tool to recognize integrins with different recognition modalities, providing novel insight on the structural requirements needed to their specific recognition.