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Analysis of hydrolyzable polyethylene glycol hydrogels and deproteinized bone mineral as delivery systems for glycosylated and non-glycosylated bone morphogenetic protein-2


Hänseler, P; Jung, U W; Jung, R E; Choi, K; Choi, K S; Hämmerle, C H F; Weber, Franz E (2012). Analysis of hydrolyzable polyethylene glycol hydrogels and deproteinized bone mineral as delivery systems for glycosylated and non-glycosylated bone morphogenetic protein-2. Acta Biomaterialia, 8(1):116-123.

Abstract

Bone morphogenetic proteins (BMP), in particular BMP-2, are the growth factors primarily responsible for osteoinduction. A knowledge of interactions between bone substitute materials and growth factor variants is crucial to designing bone substitutes with an ideal release profile. Here we compare glycosylated and non-glycosylated recombinant human bone morphogenetic protein-2 (rhBMP-2) either incorporated into a hydrolyzable polyethylene glycol (PEG) hydrogel developed as a slow release system or adsorbed to a deproteinized bovine bone matrix (DBBM), a clinically well-established bone substitute material. rhBMP-2 loaded materials were immersed in cell culture medium and rhBMP-2 concentration profiles in the supernatant were determined by an enzyme-linked immunosorbent assay. The corresponding biological activities were assessed in vitro by alkaline phosphatase activity assay. We show a strong affinity of rhBMP-2 for DBBM and reduced biological activity after its release from PEG hydrogels. Glycosylated rhBMP-2 was significantly less affected by the hydrogel and interacted significantly more strongly with DBBM than non-glycosylated rhBMP-2. We therefore question the combination of PEG hydrogels with DBBM as a rhBMP-2 delivery system over DBBM alone, since rhBMP-2 released from the hydrogel will be trapped by DBBM. Moreover, our results suggest that glycosylated rhBMP-2 is favorable in combination with PEG hydrogels, since its activity is better preserved, whereas in combination with DBBM non-glycosylated rhBMP-2 is favorable, benefiting from an initially higher concentration of free rhBMP-2.

Abstract

Bone morphogenetic proteins (BMP), in particular BMP-2, are the growth factors primarily responsible for osteoinduction. A knowledge of interactions between bone substitute materials and growth factor variants is crucial to designing bone substitutes with an ideal release profile. Here we compare glycosylated and non-glycosylated recombinant human bone morphogenetic protein-2 (rhBMP-2) either incorporated into a hydrolyzable polyethylene glycol (PEG) hydrogel developed as a slow release system or adsorbed to a deproteinized bovine bone matrix (DBBM), a clinically well-established bone substitute material. rhBMP-2 loaded materials were immersed in cell culture medium and rhBMP-2 concentration profiles in the supernatant were determined by an enzyme-linked immunosorbent assay. The corresponding biological activities were assessed in vitro by alkaline phosphatase activity assay. We show a strong affinity of rhBMP-2 for DBBM and reduced biological activity after its release from PEG hydrogels. Glycosylated rhBMP-2 was significantly less affected by the hydrogel and interacted significantly more strongly with DBBM than non-glycosylated rhBMP-2. We therefore question the combination of PEG hydrogels with DBBM as a rhBMP-2 delivery system over DBBM alone, since rhBMP-2 released from the hydrogel will be trapped by DBBM. Moreover, our results suggest that glycosylated rhBMP-2 is favorable in combination with PEG hydrogels, since its activity is better preserved, whereas in combination with DBBM non-glycosylated rhBMP-2 is favorable, benefiting from an initially higher concentration of free rhBMP-2.

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Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Center for Dental Medicine > Clinic for Fixed and Removable Prosthodontics
04 Faculty of Medicine > Center for Dental Medicine > Clinic for Cranio-Maxillofacial Surgery
04 Faculty of Medicine > University Hospital Zurich > Division of Surgical Research
Dewey Decimal Classification:610 Medicine & health
Language:English
Date:2012
Deposited On:08 Jun 2012 09:11
Last Modified:07 Dec 2017 14:20
Publisher:Elsevier
ISSN:1742-7061
Publisher DOI:https://doi.org/10.1016/j.actbio.2011.08.002
PubMed ID:21867781

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