Supramolecular Platform Stabilizing Growth Factors
Author(s) -
Simone I. S. Hendrikse,
Sergio Spaans,
E. W. Meijer,
Patricia Y. W. Dankers
Publication year - 2018
Publication title -
biomacromolecules
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.689
H-Index - 220
eISSN - 1526-4602
pISSN - 1525-7797
DOI - 10.1021/acs.biomac.8b00219
Subject(s) - supramolecular chemistry , supramolecular polymers , chemistry , excipient , biophysics , transforming growth factor , polymer , in vivo , growth factor , combinatorial chemistry , molecule , biochemistry , receptor , microbiology and biotechnology , organic chemistry , chromatography , biology
High concentrations of supplemented growth factors can cause oversaturation and adverse effects in in vitro and in vivo studies, though these supraphysiological concentrations are often required due to the low stability of growth factors. Here we demonstrate the stabilization of TGF-β1 and BMP4 using supramolecular polymers. Inspired by heparan sulfate, sulfonated peptides were presented on a supramolecular polymer to allow for noncovalent binding to growth factors in solution. After mixing with excipient molecules, both TGF-β1 and BMP4 were shown to have a prolonged half-life compared to the growth factors free in solution. Moreover, high cellular response was measured by a luciferase assay, indicating that TGF-β1 remained highly active upon binding to the supramolecular assembly. The results demonstrate that significant lower concentrations of growth factors can be used when supramolecular polymers bearing growth factor binding moieties are implemented. This approach can also be exploited in hydrogel systems to control growth factor release.
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