Start Publications Construction and hemocompatibility study of highly bioactive ...
QSense

Construction and hemocompatibility study of highly bioactive heparin-functionalized surface†

Year: 2012

Journal: Journal of Biomedical Materials Research Part A Volume 100A, Issue 11, pages 3124–3133, November 2012, 20130119

Authors: Zhi-Lu Yang 1 2 ‡, Shuo Zhou 1 ‡, Lei Lu 1, Xin Wang 1, Jin Wang 1 *, Nan Huang 1 2 *

Last authors: Nan Huang

Organizations: 1 
Key Laboratory of Advanced Technology for Materials of Education Ministry, Southwest Jiaotong University, Chengdu 610031, China 2
 The Institute of Biomaterials and Surface Engineering, Southwest Jiaotong University, Chengdu 610031, China ‡
These authors contributed equally to this work.
 Email: Jin Wang (jinxxwang@263.net), Nan Huang (nhuang@263.net) *Key Laboratory of Advanced Technology for Materials of Education Ministry, Southwest Jiaotong University, Chengdu 610031, China †
How to cite this article: Yang Z-L, Zhou S, Lu L, Wang X, Wang J, Huang N. 2012. Construction and hemocompatibility study of highly bioactive heparin-functionalized surface. J Biomed Mater Res Part A 2012:100A:3124–3133.
 ‡
These authors contributed equally to this work.

Country: china

A simple method is developed to construct anticoagulant surfaces via passive adsorption of heparin onto the protonated plasma-polymerized allylamine (PPAam) films from phosphate-buffered saline (PBS). These protonated PPAam surfaces are found to have high affinity to heparin. Importantly, the heparin-functionalized PPAam (Hep–PPAam) surfaces show good retention of heparin after long-term immersion in PBS. The Hep–PPAam surface prolongs the activated partial thromboplastin time for about 20 s as compared to 316L stainless steel even though the adsorption amount of heparin is only about 300 ng/cm2. This indicates that the heparin bound to the protonated PPAam surfaces in this way maintains a high bioactivity. Blood platelet adhesion and activation on this surface is remarkably reduced and adsorption and activation of fibrinogen is inhibited. Thus, Hep–PPAam surface modification leads to a significant improve of the hemocompatibility. © 2012 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 100A:3124–3133, 2012.