Crosslinking of collagen with dendrimers

Journal of Biomedical Materials Research - Part A - Tập 75A Số 3 - Trang 510-518 - 2005
Xiaodong Duan1, Heather Sheardown1
1Department of Chemical Engineering, McMaster University, 1280 Main St. W., Hamilton, Ontario, L8S 4L7, Canada

Tóm tắt

AbstractPolypropyleneimine octaamine dendrimers were studied as an alternative means of generating highly crosslinked collagen. Crosslinking was effected by using the water‐soluble carbodiimide 1‐ethyl‐3‐(3‐dimethyl aminopropyl) carbodiimide hydrochloride (EDC). The multifunctional dendrimers were introduced as novel crosslinkers after the activation of the carboxylic acid groups of glutamic and aspartic acid residues in collagen. The conventional crosslinker glutaraldehyde was used as a control. EDC, itself an alternative crosslinker, which forms zero‐length crosslinks by directly covalently binding collagen molecules, as well as a low molecular weight diamine and a low molecular weight triamine, were also studied. All of the resultant gels were freeze‐dried to obtain sponges for characterization. Water uptake of the gels decreased from 90% to 60% after dendrimer crosslinking compared with EDC crosslinking. DSC results showed an increase of denaturation temperature of collagen after crosslinking with the various methods. The generation 2 and 3 dendrimer‐crosslinked collagen samples had the highest denaturation temperature, at up to 90°C compared with 50°C in the uncrosslinked collagen control. The dendrimer‐crosslinked collagen also showed unique thermal characteristics, with multiple denaturation temperature peaks in contrast to the single peak noted with the other crosslinked collagens. This is thought to be due to the heterogeneous nature of dendrimer crosslinking. Collagenase results revealed that the dendrimer‐crosslinked collagen had a comparative resistance to proteolysis to glutaraldehyde‐crosslinked collagen. Measurement of activated carboxylic acid groups before and after crosslinking indicated that 40–70% of the activated carboxylic acid was consumed during crosslinking with dendrimers. The results suggest that dendrimer crosslinking of collagen produces stable gels. The presence of a large number of excess amine groups in the dendrimers may also be useful for subsequent modification with biologically relevant groups. © 2005 Wiley Periodicals, Inc. J Biomed Mater Res, 2005

Từ khóa


Tài liệu tham khảo

10.1016/j.addr.2003.08.008

10.1016/j.addr.2003.08.003

10.1016/j.addr.2003.08.004

10.1016/S1084952102000940

10.1016/S0378-5173(01)00691-3

10.1016/S0168-3659(01)00467-9

10.1016/S0142-9612(02)00067-4

10.1097/01.ico.0000263120.68768.f8

10.1159/000028064

10.1073/pnas.2536767100

10.1002/jbm.820221008

10.1007/BF00119733

10.1016/S0142-9612(98)00242-7

10.3349/ymj.2001.42.2.172

10.1016/S0142-9612(96)00106-8

10.1016/S0142-9612(01)00067-9

10.1002/jbm.820140607

10.1002/jbm.a.10082

10.1002/jbm.820280204

10.1002/1097-4636(2001)58:2<172::AID-JBM1004>3.0.CO;2-9

Girardot JMD, 1996, Amide cross‐linking: an alternative to glutaraldehyde fixation, J Heart Valve Dis, 5, 518

10.1002/(SICI)1097-4636(199610)32:2<209::AID-JBM9>3.0.CO;2-X

10.1007/BF02522870

10.1016/j.biomaterials.2003.09.092

10.1016/0142-9612(96)82721-9

10.1016/j.biomaterials.2004.07.063

Thông tin
Thông tin xuất bản

Journal of Biomedical Materials Research - Part A

Tập 75A Số 3

510-518

Thông tin tác giả