文献类型：期刊文献

英文题名：Enhanced osteogenesis of bone morphology protein-2 in 2-N,6-O-sulfated chitosan immobilized PLGA scaffolds

作者：Kong, Xiangjun[3];Wang, Jing[3];Cao, Lingyan[3];Yu, Yuanman[3];Liu, Changsheng[1,2,3]

机构：[1]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]E China Univ Sci & Technol, Minist Educ, Key Lab Ultrafine Mat, Shanghai 200237, Peoples R China;[3]E China Univ Sci & Technol, Minist Educ, Engn Res Ctr Biomed Mat, Shanghai 200237, Peoples R China

年份：2014

卷号：122

起止页码：359

外文期刊名：COLLOIDS AND SURFACES B-BIOINTERFACES

收录：;EI(收录号：20144600211439);WOS:【SCI-EXPANDED(收录号:WOS:000343612900045)】；

基金：The authors are indebted to the financial support from the National Basic Research Program of China (973 Program, 2012CB933600), the National Natural Science Foundation of China (Nos. 31273011 and 31330028), the National Science and Technology Support Program (2012BAI17B02), and the Program for New Century Excellent Talents in University (NCET-12-0856).

语种：英文

外文关键词：Scaffold; Surface modification; Sulfated chitosan; Bone morphology protein-2; Osteogenesis

摘要：By using 2-N,6-O-sulfated chitosan (26SCS) immobilized poly(lactide-co-glycolide) (PLGA) scaffolds, our system achieved controlled release and improved bioactivity of recombinant human bone morphology protein-2 (rhBMP-2). Initially aminolyzed by ethylenediamine, PLGA scaffolds surface was immobilized with 26SCS via electrostatic assembly. Upon the presence of 26SCS, the system displayed improved rhBMP-2 adsorption and prolonged release process in vitro due to the high affinity of rhBMP-2 with 26SCS. On the other hand, because of incorporation of 26SCS, the system appeared to be more hydrophilic and provided a better environment for cells attachment. Moreover, 26SCS enhanced the binding efficiency between rhBMP-2 and its receptors as well as alkaline phosphatase activity. Our study highlights 26SCS immobilized PLGA scaffolds may be excellent candidates for use in bone tissue engineering. (C) 2014 Elsevier B.V. All rights reserved.