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Osteogenic properties of a short BMP ‐2 chimera peptide
Author(s) -
Falcigno Lucia,
D'Auria Gabriella,
Calvanese Luisa,
Marasco Daniela,
Iacobelli Roberta,
Scognamiglio Pasqualina L.,
Brun Paola,
Danesin Roberta,
Pasqualin Matteo,
Castagliuolo Ignazio,
Dettin Monica
Publication year - 2015
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2793
Subject(s) - chimera (genetics) , peptide , bone morphogenetic protein 2 , chemistry , microbiology and biotechnology , biochemistry , biology , gene , in vitro
Bone morphogenetic proteins (BMPs) play a key role in bone and cartilage formation. For these properties, BMPs are employed in the field of tissue engineering to induce bone regeneration in damaged tissues. To overcome drawbacks due to the use of entire proteins, synthetic peptides derived from their parent BMPs have come out as promising molecules for biomaterial design. On the structural ground of the experimental BMP‐2 receptor complexes reported in the literature, we designed three peptides, reproducing the BMP‐2 region responsible for the binding to the type II receptor, ActRIIB. These peptides were characterized by NMR, and the structural features of the peptide–receptor binding interface were highlighted by docking experiments. Peptide–receptor binding affinities were analyzed by means of ELISA and surface plasmon resonance techniques. Furthermore, cellular assays were performed to assess their osteoinductive properties. A chimera peptide, obtained by combining the sequence portions 73–92 and 30–34 of BMP‐2, shows the best affinity for ActRIIB in the series and represents a good starting point for the design of new compounds able to reproduce osteogenic properties of the parent BMP‐2. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.