Protein-polymer conjugates for forming photopolymerizable biomimetic hydrogels for tissue engineering

被引:115
作者
Gonen-Wadmany, Maya [1 ]
Oss-Ronen, Liat [1 ]
Seliktar, Dror [1 ]
机构
[1] Technion Israel Inst Technol, Fac Biomed Engn, IL-32000 Haifa, Israel
基金
以色列科学基金会;
关键词
albumin; fibrin; collagen; poly(ethylene glycol); scaffold; smooth muscle cells;
D O I
10.1016/j.biomaterials.2007.05.005
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
Collagen, fibrin and albumin are popular proteins for making biological scaffolds for tissue engineering because of their biocompatibility, biodegradability, and availability. A major drawback of biological protein-based biomaterials is the limited control over their physical and biodegradation properties. Our laboratory has been developing new protein-based biomaterials with tunable properties without the use of cytotoxic protein cross-linking techniques. We describe the formation and assembly of photopolymerizable biomimetic hydrogel scaffolds made from protein polymer conjugates of poly(ethylene glycol) (PEG) and collagen, fibrin or albumin. The conjugation of PEG to these proteins (PEGylation) was verified by SDS-PAGE and the polymerization reaction into a hydrogel network was confirmed by shear rheometry. The differences in rheology and swelling characteristics of the three hydrogel materials underscore the importance of the molecular relationship between the PEG and the protein constituent in this protein-polymer arrangement. The biofunctionality of the PEGylated collagen and fibrinogen hydrogels sustained both cell adhesion and proteolytic degradation that enabled 3-D cell spreading and migration within the hydrogel network. PEG albumin hydrogels exhibited poor cell spreading and migration by virtue of the fact that the albumin backbone lacks any known cell adhesion sites. Despite differences in the biological and structural composition of the PEGylated fibrinogen and collagen hydrogels, the rate of cellular migration within each material was not significantly different. (c) 2007 Elsevier Ltd. All rights reserved.
引用
收藏
页码:3876 / 3886
页数:11
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