期刊
ACTA BIOMATERIALIA
卷 8, 期 6, 页码 2144-2152出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.actbio.2012.03.021
关键词
Transforming growth factor-beta 1 (TGF-beta 1); Chondroitin sulfate derivatives; Hyaluronic acid/hyaluronan derivatives; Surface plasmon resonance; ELISA
资金
- DFG [PAK 105, TRR 67, A3]
This study demonstrates that the modification of hyaluronan (hyaluronic acid; Hya) and chondroitin sulfate (CS) with sulfate groups leads to different binding affinities for recombinant human transforming growth factor-beta 1 (TGF-beta 1) for comparable average degrees of sulfation (DS). In general, Hya derivates showed higher binding strength than CS derivatives. In either case, a higher degree of sulfation leads to a stronger interaction. The high-sulfated hyaluronan sHya3 (average DS approximate to 3) exhibited the tightest interaction with TGF-beta 1, as determined by surface plasmon resonance and enzyme-linked immunosorbent assay. The binding strength was significantly weakened by carboxymethylation. Unmodified Hya and low-sulfated, native CS showed weak or no binding affinity. The interaction characteristics of the different sulfated glycosaminoglycans are promising for incorporation into bioengineered coatings of biomaterials to modulate growth factor binding in medical applications. (C) 2012 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.
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