Biomineralization on single crystalline rutile: the modulated growth of hydroxyapatite by fibronectin in a simulated body fluid. Issue 42 (12th April 2016)
- Record Type:
- Journal Article
- Title:
- Biomineralization on single crystalline rutile: the modulated growth of hydroxyapatite by fibronectin in a simulated body fluid. Issue 42 (12th April 2016)
- Main Title:
- Biomineralization on single crystalline rutile: the modulated growth of hydroxyapatite by fibronectin in a simulated body fluid
- Authors:
- Cai, Yixiao
Li, Hu
Karlsson, Mikael
Leifer, Klaus
Engqvist, Håkan
Xia, Wei - Abstract:
- Abstract : The aim of this study is to probe the complex interaction between surface bioactivity and protein adsorption on single crystalline rutile. Abstract : The aim of this study is to probe the complex interaction between surface bioactivity and protein adsorption on single crystalline rutile. Our previous studies have shown that single crystalline rutile possessed in vitro bioactivity and the crystalline faces affected the hydroxyapatite (HA) formation. However, upon implantation, a fast adsorption of proteins, from the biological fluids, is intermediated by a water layer towards the biomaterial interface. Thus the effect of protein on the bioactivity must be addressed. In this study, the HA growth dynamics on (001), (100) and (110) faces was investigated in a simulated body fluid with the presence of fibronectin (FN) by two different processes. The surface adhesion of each face before and after FN adsorption, as revealed by direct numerical values, was determined by atomic force microscopy (AFM) based peak force quantitative nanomechanical mapping (PF-QNM) for the first time. The findings suggest the surface energies of FN pre-adsorbed (001), (100) and (110) faces have been enhanced, leading to the subsequent accelerated HA formation. Furthermore, (001) and (100) faces were found to have larger coverage of HA crystals than (110) face at an early stage. In addition, various characterizations were performed to probe the chemical and crystal structures of as-grownAbstract : The aim of this study is to probe the complex interaction between surface bioactivity and protein adsorption on single crystalline rutile. Abstract : The aim of this study is to probe the complex interaction between surface bioactivity and protein adsorption on single crystalline rutile. Our previous studies have shown that single crystalline rutile possessed in vitro bioactivity and the crystalline faces affected the hydroxyapatite (HA) formation. However, upon implantation, a fast adsorption of proteins, from the biological fluids, is intermediated by a water layer towards the biomaterial interface. Thus the effect of protein on the bioactivity must be addressed. In this study, the HA growth dynamics on (001), (100) and (110) faces was investigated in a simulated body fluid with the presence of fibronectin (FN) by two different processes. The surface adhesion of each face before and after FN adsorption, as revealed by direct numerical values, was determined by atomic force microscopy (AFM) based peak force quantitative nanomechanical mapping (PF-QNM) for the first time. The findings suggest the surface energies of FN pre-adsorbed (001), (100) and (110) faces have been enhanced, leading to the subsequent accelerated HA formation. Furthermore, (001) and (100) faces were found to have larger coverage of HA crystals than (110) face at an early stage. In addition, various characterizations were performed to probe the chemical and crystal structures of as-grown biomimetic HA crystals, and in particular, the Ca/P ratio variations at different soaking time points. … (more)
- Is Part Of:
- RSC advances. Volume 6:Issue 42(2016)
- Journal:
- RSC advances
- Issue:
- Volume 6:Issue 42(2016)
- Issue Display:
- Volume 6, Issue 42 (2016)
- Year:
- 2016
- Volume:
- 6
- Issue:
- 42
- Issue Sort Value:
- 2016-0006-0042-0000
- Page Start:
- 35507
- Page End:
- 35516
- Publication Date:
- 2016-04-12
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c6ra04303h ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 1924.xml