journal article·2014-12-24

Sustained Immobilization of Growth Factor Proteins Based on Functionalized Parylenes

Yung-Chih Chen, Ting-Pi Sun, Chiao-Tzu Su, Jyun-Ting Wu, Chih-Yeh Lin, Jiashing Yu, Chao-Wei Huang, Chia-Jie Chen, Hsien-Yeh Chen

Publisher page

Abstract

Protein molecules immobilized on biomaterial surfaces are performed based on oriented conjugation or replaced mimicking peptides. The sustainable immobilization of growth factor proteins using functionalized parylene coatings is demonstrated in this study. Site-specific and nonspecific immobilization approaches are realized to conjugate bone morphogenetic protein (BMP-2). The binding affinities and conformational changes of BMP-2 are confirmed by QCM and SPR characterizations. Osteoinduction of stem cells is examined by ALP activity on the BMP-2 modified surfaces. Finally, immobilizations and equally sustained biological functions of vascular endothelial growth factor (VEGF) and a mimicking peptide of KLTWQELYQLKYKG (QK) are also examined and confirmed.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Nanofabrication and Lithography Techniques · Molecular Junctions and Nanostructures · Biochemical and Structural Characterization

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Department of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan

Department of Animal Science and Technology, National Taiwan University, Taipei 10617, Taiwan

Department of Orthopedic Surgery, National Taiwan University, Taipei 10018, Taiwan

Funding

National Science Council Taiwan

References (30)

Show source-provided references
1. Talbert J. N. · Colloids Surf., B · 2012 · 93 · 810.1016/j.colsurfb.2012.01.003 ↗
2. Valeur E. · Chem. Soc. Rev. · 2009 · 38 · 60610.1039/B701677H ↗
3. Hermanson G. T. · 2008
4. Sletten E. M. · Angew. Chem., Int. Ed. · 2009 · 48 · 697410.1002/anie.200900942 ↗
5. Ito Y. · Biomaterials · 2013 · 34 · 756510.1016/j.biomaterials.2013.06.037 ↗
6. Secundo F. · Chem. Soc. Rev. · 2013 · 42 · 625010.1039/c3cs35495d ↗
7. Wong L. S. · J. Am. Chem. Soc. · 2008 · 130 · 1245610.1021/ja8030278 ↗
8. Masters K. S. · Macromol. Biosci. · 2011 · 11 · 114910.1002/mabi.201000505 ↗
9. Liberelle B. t. · Bioconjugate Chem. · 2010 · 21 · 225710.1021/bc1002604 ↗
10. Chen H.-Y. · Langmuir · 2010 · 27 · 3410.1021/la101623n ↗
11. Chen H.-Y. · J. Am. Chem. Soc. · 2010 · 132 · 1802310.1021/ja108679m ↗
12. Wu J.-T. · Macromol. Rapid Commun. · 2012 · 33 · 92210.1002/marc.201200011 ↗
13. Singh R. · Anal. Biochem. · 2002 · 304 · 14710.1006/abio.2002.5624 ↗
14. Sun M. M. C. · Bioconjugate Chem. · 2005 · 16 · 128210.1021/bc050201y ↗
15. Mädler S. · J. Mass Spectrom. · 2009 · 44 · 69410.1002/jms.1544 ↗
16. Tsai M.-Y. · Chem. Commun. · 2012 · 48 · 1096910.1039/c2cc35892a ↗
17. Marx K. A. · Biomacromolecules · 2003 · 4 · 109910.1021/bm020116i ↗
18. Rickert J. · Anal. Chem. · 1997 · 69 · 144110.1021/ac960875p ↗
19. Han H.-C. · Biosens. Bioelectron. · 2009 · 24 · 154310.1016/j.bios.2008.07.033 ↗
20. Sauerbrey G. · Z. Physik · 1959 · 155 · 20610.1007/BF01337937 ↗
21. Zaera F. · Chem. Rev. · 2012 · 112 · 292010.1021/cr2002068 ↗
22. Hedin J. · Langmuir · 2007 · 23 · 614810.1021/la063406j ↗
23. Vörös J. · Biophys. J. · 2004 · 87 · 55310.1529/biophysj.103.030072 ↗
24. Kim S. E. · Biomaterials · 2011 · 32 · 36610.1016/j.biomaterials.2010.09.008 ↗
25. Kim Y.-J. · J. Biol. Chem. · 2004 · 279 · 5077310.1074/jbc.M404145200 ↗
26. Otvos L. · 2008 · 110.1007/978-1-59745-419-3 ↗
27. D’Andrea L. D. · Proc. Natl. Acad. Sci. U.S.A. · 2005 · 102 · 1421510.1073/pnas.0505047102 ↗
28. Leslie-Barbick J. E. · Biomaterials · 2011 · 32 · 578210.1016/j.biomaterials.2011.04.060 ↗
29. Valenzuela C. D. · Tissue Eng., Part A · 2013 · 19 · 137310.1089/ten.tea.2012.0323 ↗