Premium
Engineering a VEGF fusion protein for use with an artificial extracellular matrix with programmable binding affinities
Author(s) -
Elliott Robert,
Barkas Aleeza,
Balog Eva Rose
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.798.12
Subject(s) - fusion protein , extracellular matrix , affinities , vascular endothelial growth factor , chemistry , sh3 domain , extracellular , computational biology , elastin , microbiology and biotechnology , vegf receptors , biology , proto oncogene tyrosine protein kinase src , biochemistry , signal transduction , genetics , cancer research , gene , recombinant dna
We are interested in novel protein biomaterials that recapitulate the natural chemical and physical signals employed by the body to manage and inform blood vessel regulation. Despite great advances in artificial extracellular matrices (aECMs) for controlled presentation and release of Vascular Endothelial Growth Factor (VEGF), these materials still fall short of the incredibly complex dynamic signaling of the natural extracellular matrix. Here we show the molecular cloning and bacterial expression of a VEGF fusion protein composed of a soluble VEGF isoform and the protein domain Src Homology 3 (SH3). When combined with an aECM possessing SH3 binding peptides of variable affinity, this novel fusion protein will allow us to study the effects of ECM‐binding on VEGF signaling. Toward this goal we have also designed and synthesized a mini‐suite of elastin‐like polymers (ELPs) with various SH3‐binding sites for incorporation into 2‐D or 3‐D aECMs. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .